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Conserved domains on  [gi|239938634|sp|P28264|]
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RecName: Full=Cell division protein FtsA

Protein Classification

cell division protein FtsA( domain architecture ID 11436667)

cell division protein FtsA may serve as a membrane anchor for the Z ring

CATH:  3.30.420.40|3.90.640.10|3.30.1490.110
Gene Ontology:  GO:0051301|GO:0043093
PubMed:  22473211

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FtsA COG0849
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
2-381 8.24e-179

Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 440610 [Multi-domain]  Cd Length: 402  Bit Score: 505.05  E-value: 8.24e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   2 NNNELYVSLDIGTSNTKVIVGEMTDD-SLNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVN 80
Cdd:COG0849    1 AKSNIIVGLDIGTSKVVALVGEVDPDgKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  81 GNYINIQDTNGVVAVSseNKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLIT 160
Cdd:COG0849   81 GGHIKSQNSRGVVAIS--GREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIVT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 161 GSKTILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKD 240
Cdd:COG0849  159 GPKTAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITND 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 241 ISIGLRTSTEEAERVKKQLGHAYYDEASEDEIFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSEELRSMGITD-LP 319
Cdd:COG0849  239 IAIGLRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKELKRSGYEEkLP 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239938634 320 GGFVLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIG-----VRDPQYMTGVGLIQFACRNARIQGRK 381
Cdd:COG0849  319 AGVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGglpeaVRDPAYATAVGLLLYAAKNQEERFEP 385
 
Name Accession Description Interval E-value
FtsA COG0849
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
2-381 8.24e-179

Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440610 [Multi-domain]  Cd Length: 402  Bit Score: 505.05  E-value: 8.24e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   2 NNNELYVSLDIGTSNTKVIVGEMTDD-SLNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVN 80
Cdd:COG0849    1 AKSNIIVGLDIGTSKVVALVGEVDPDgKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  81 GNYINIQDTNGVVAVSseNKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLIT 160
Cdd:COG0849   81 GGHIKSQNSRGVVAIS--GREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIVT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 161 GSKTILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKD 240
Cdd:COG0849  159 GPKTAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITND 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 241 ISIGLRTSTEEAERVKKQLGHAYYDEASEDEIFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSEELRSMGITD-LP 319
Cdd:COG0849  239 IAIGLRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKELKRSGYEEkLP 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239938634 320 GGFVLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIG-----VRDPQYMTGVGLIQFACRNARIQGRK 381
Cdd:COG0849  319 AGVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGglpeaVRDPAYATAVGLLLYAAKNQEERFEP 385
ftsA TIGR01174
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ...
 6-370 3.63e-171

cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the bacterial homolog of tubulin. It is an ATP-binding protein and shows structural similarities to actin and heat shock cognate protein 70. [Cellular processes, Cell division]


Pssm-ID: 273483 [Multi-domain]  Cd Length: 371  Bit Score: 484.45  E-value: 3.63e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634    6 LYVSLDIGTSNTKVIVGEMTDDS-LNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNYI 84
Cdd:TIGR01174   1 LIVGLDIGTSKICAIVAEVLEDGeLNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   85 NIQDTNGVVAVSSenKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSKT 164
Cdd:TIGR01174  81 KSQNSIGVVAIKD--KEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVRLEVEVHIITGSST 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  165 ILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIG 244
Cdd:TIGR01174 159 ILRNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  245 LRTSTEEAERVKKQLGHAYYDEASEDEIFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVS-EELRSMGI-TDLPGGF 322
Cdd:TIGR01174 239 LRTPLEEAERIKIKYGCASIPLEGPDENIEIPSVGERPPRSLSRKELAEIIEARAEEILEIVKqKELRKSGFkEELNGGI 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 239938634  323 VLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIG-----VRDPQYMTGVGLIQF 370
Cdd:TIGR01174 319 VLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGgltedVNDPEYSTAVGLLLY 371
ASKHA_NBD_FtsA cd24048
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ...
 5-370 4.24e-165

nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.


Pssm-ID: 466898 [Multi-domain]  Cd Length: 372  Bit Score: 468.93  E-value: 4.24e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   5 ELYVSLDIGTSNTKVIVGEMT-DDSLNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNY 83
Cdd:cd24048    1 NIIVGLDIGTSKICALVGEVSeDGELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  84 INIQDTNGVVAVSSENkEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSK 163
Cdd:cd24048   81 IRSVNSRGVIAISDKD-EITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGSRLEVDVHVITGSS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 164 TILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISI 243
Cdd:cd24048  160 SAIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 244 GLRTSTEEAERVKKQLGHAYYDEASEDEIFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSEELRSMGITD-LPGGF 322
Cdd:cd24048  240 GLNTPFEEAERLKIKYGSALSEEADEDEIIEIPGVGGREPREVSRRELAEIIEARVEEILELVKKELKESGYEDlLPGGI 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 239938634 323 VLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIG-----VRDPQYMTGVGLIQF 370
Cdd:cd24048  320 VLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGglpeeVNDPAYATAVGLLLY 372
ftsA PRK09472
cell division protein FtsA; Reviewed
 6-371 7.67e-75

cell division protein FtsA; Reviewed


Pssm-ID: 181887 [Multi-domain]  Cd Length: 420  Bit Score: 240.07  E-value: 7.67e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   6 LYVSLDIGTSNTKVIVGEMTDDS-LNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNYI 84
Cdd:PRK09472   9 LVVGLEIGTAKVAALVGEVLPDGmVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  85 NIQDTNGVVAVSSEnkEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSKT 164
Cdd:PRK09472  89 SCQNEIGMVPISEE--EVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHND 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 165 ILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIG 244
Cdd:PRK09472 167 MAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 245 LRTSTEEAERVKKQLGHAYYDEASEDEIFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSEE-------LRSMGIT- 316
Cdd:PRK09472 247 FGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEilqlqeqLRQQGVKh 326

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 317 DLPGGFVLTGGQAAMPGVMSLAQDVLQNNVRVASP-NYIG----VRDPQYMTGVGLIQFA 371
Cdd:PRK09472 327 HLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPlNITGltdyAQEPYYSTAVGLLHYG 386
FtsA smart00842
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
 7-194 1.28e-72

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains.


Pssm-ID: 214850  Cd Length: 187  Bit Score: 226.20  E-value: 1.28e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634     7 YVSLDIGTSNTKVIVGEMTDD-SLNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNYIN 85
Cdd:smart00842   1 IVGLDIGTSKIKALVAEVDEDgEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634    86 IQDTNGVVAVssENKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSKTI 165
Cdd:smart00842  81 SVNVSGVVAI--PDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVRLEVDVHVVTAPKSA 158

                          170       180
                   ....*....|....*....|....*....
gi 239938634   166 LHNLLRCVERAGIEITDICLQPLAAGSAA 194
Cdd:smart00842 159 IQNLEKCVERAGLEVDGIVLEPLASAEAV 187
FtsA pfam14450
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
 205-366 3.57e-53

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.


Pssm-ID: 464177 [Multi-domain]  Cd Length: 167  Bit Score: 175.60  E-value: 3.57e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  205 ALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIGLRTSTEEAERVKKQLGHAYYDEASEDeifEVTVIGTNQKQ 284
Cdd:pfam14450   1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADED---EVPGVGGREPR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  285 TFTQQEAANIIEARVEEILEIVSEELRSMG--------ITDLPGGFVLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIGV 356
Cdd:pfam14450  78 EISRKELAEIIEARVEEILELVRAELEDREvlpgeyvrLEVDVHGIVLTGGGSALPGLVELAERALGLPVRIGSPDGIGG 157

                         170
                  ....*....|
gi 239938634  357 RDPQYMTGVG 366
Cdd:pfam14450 158 RNPAYATALG 167
 
Name Accession Description Interval E-value
FtsA COG0849
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
2-381 8.24e-179

Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440610 [Multi-domain]  Cd Length: 402  Bit Score: 505.05  E-value: 8.24e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   2 NNNELYVSLDIGTSNTKVIVGEMTDD-SLNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVN 80
Cdd:COG0849    1 AKSNIIVGLDIGTSKVVALVGEVDPDgKLEVIGVGEAPSRGVKKGVIVDIEATVEAIRKAVEEAERMAGVKIESVYVGIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  81 GNYINIQDTNGVVAVSseNKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLIT 160
Cdd:COG0849   81 GGHIKSQNSRGVVAIS--GREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEVDVHIVT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 161 GSKTILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKD 240
Cdd:COG0849  159 GPKTAVQNLVKCVERAGLEVEDLVLSPLASAEAVLTEDEKELGVALVDIGGGTTDIAVFKDGALRHTAVIPVGGDHITND 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 241 ISIGLRTSTEEAERVKKQLGHAYYDEASEDEIFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSEELRSMGITD-LP 319
Cdd:COG0849  239 IAIGLRTPLEEAERLKIKYGSALASLADEDETIEVPGIGGRPPREISRKELAEIIEARVEEIFELVRKELKRSGYEEkLP 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239938634 320 GGFVLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIG-----VRDPQYMTGVGLIQFACRNARIQGRK 381
Cdd:COG0849  319 AGVVLTGGGSQLPGLVELAEEILGLPVRIGRPDGIGglpeaVRDPAYATAVGLLLYAAKNQEERFEP 385
ftsA TIGR01174
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ...
 6-370 3.63e-171

cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the bacterial homolog of tubulin. It is an ATP-binding protein and shows structural similarities to actin and heat shock cognate protein 70. [Cellular processes, Cell division]


Pssm-ID: 273483 [Multi-domain]  Cd Length: 371  Bit Score: 484.45  E-value: 3.63e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634    6 LYVSLDIGTSNTKVIVGEMTDDS-LNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNYI 84
Cdd:TIGR01174   1 LIVGLDIGTSKICAIVAEVLEDGeLNIIGVGTHPSRGIKKGVINDIEAAVGSIQRAIEAAELMAGCEIRSVIVSISGAHI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   85 NIQDTNGVVAVSSenKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSKT 164
Cdd:TIGR01174  81 KSQNSIGVVAIKD--KEVTQEDIERVLETAKAVAIPNDQEILHVIPQEYILDDQEGIKNPLGMSGVRLEVEVHIITGSST 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  165 ILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIG 244
Cdd:TIGR01174 159 ILRNLVKCVERCGLEVDNIVLSGLASAIAVLTEDEKELGVCLIDIGGGTTDIAVYTGGSIRYTKVIPIGGNHITKDIAKA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  245 LRTSTEEAERVKKQLGHAYYDEASEDEIFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVS-EELRSMGI-TDLPGGF 322
Cdd:TIGR01174 239 LRTPLEEAERIKIKYGCASIPLEGPDENIEIPSVGERPPRSLSRKELAEIIEARAEEILEIVKqKELRKSGFkEELNGGI 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 239938634  323 VLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIG-----VRDPQYMTGVGLIQF 370
Cdd:TIGR01174 319 VLTGGGAQLEGIVELAEKVFDNPVRIGLPQNIGgltedVNDPEYSTAVGLLLY 371
ASKHA_NBD_FtsA cd24048
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ...
 5-370 4.24e-165

nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.


Pssm-ID: 466898 [Multi-domain]  Cd Length: 372  Bit Score: 468.93  E-value: 4.24e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   5 ELYVSLDIGTSNTKVIVGEMT-DDSLNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNY 83
Cdd:cd24048    1 NIIVGLDIGTSKICALVGEVSeDGELEVIGVGTVPSRGIKKGVIVDLEEAVESIRKAIEEAERMAGVKIDSVYVGISGKH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  84 INIQDTNGVVAVSSENkEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSK 163
Cdd:cd24048   81 IRSVNSRGVIAISDKD-EITEEDVERVIEAAKAVALPEDREILHVIPQEYIVDGQDGIKDPVGMSGSRLEVDVHVITGSS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 164 TILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISI 243
Cdd:cd24048  160 SAIQNLIKCVERAGLEVDDIVLSPLASAEAVLTEDEKELGVALIDIGGGTTDIAVFKNGSLRYTAVIPVGGNHITNDIAI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 244 GLRTSTEEAERVKKQLGHAYYDEASEDEIFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSEELRSMGITD-LPGGF 322
Cdd:cd24048  240 GLNTPFEEAERLKIKYGSALSEEADEDEIIEIPGVGGREPREVSRRELAEIIEARVEEILELVKKELKESGYEDlLPGGI 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 239938634 323 VLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIG-----VRDPQYMTGVGLIQF 370
Cdd:cd24048  320 VLTGGGSQLPGLVELAEEVFGMPVRIGRPKNIGglpeeVNDPAYATAVGLLLY 372
ftsA PRK09472
cell division protein FtsA; Reviewed
 6-371 7.67e-75

cell division protein FtsA; Reviewed


Pssm-ID: 181887 [Multi-domain]  Cd Length: 420  Bit Score: 240.07  E-value: 7.67e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   6 LYVSLDIGTSNTKVIVGEMTDDS-LNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNYI 84
Cdd:PRK09472   9 LVVGLEIGTAKVAALVGEVLPDGmVNIIGVGSCPSRGMDKGGVNDLESVVKCVQRAIDQAELMADCQISSVYLALSGKHI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  85 NIQDTNGVVAVSSEnkEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSKT 164
Cdd:PRK09472  89 SCQNEIGMVPISEE--EVTQEDVENVVHTAKSVRVRDEHRILHVIPQEYAIDYQEGIKNPVGLSGVRMQAKVHLITCHND 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 165 ILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIG 244
Cdd:PRK09472 167 MAKNIVKAVERCGLKVDQLIFAGLASSYAVLTEDERELGVCVVDIGGGTMDIAVYTGGALRHTKVIPYAGNVVTSDIAYA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 245 LRTSTEEAERVKKQLGHAYYDEASEDEIFEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSEE-------LRSMGIT- 316
Cdd:PRK09472 247 FGTPPSDAEAIKVRHGCALGSIVGKDESVEVPSVGGRPPRSLQRQTLAEVIEPRYTELLNLVNEEilqlqeqLRQQGVKh 326

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 317 DLPGGFVLTGGQAAMPGVMSLAQDVLQNNVRVASP-NYIG----VRDPQYMTGVGLIQFA 371
Cdd:PRK09472 327 HLAAGIVLTGGAAQIEGLAACAQRVFHTQVRIGAPlNITGltdyAQEPYYSTAVGLLHYG 386
FtsA smart00842
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
 7-194 1.28e-72

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains.


Pssm-ID: 214850  Cd Length: 187  Bit Score: 226.20  E-value: 1.28e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634     7 YVSLDIGTSNTKVIVGEMTDD-SLNIIGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGVNGNYIN 85
Cdd:smart00842   1 IVGLDIGTSKIKALVAEVDEDgEINVIGVGEVPSRGIRKGVIVDIEAAARAIREAVEEAERMAGVKIDSVYVGISGRHLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634    86 IQDTNGVVAVssENKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLITGSKTI 165
Cdd:smart00842  81 SVNVSGVVAI--PDKEITQEDIDRVLEAAKAVALPPDREILHVLPQEYILDGQEGIKDPIGMSGVRLEVDVHVVTAPKSA 158

                          170       180
                   ....*....|....*....|....*....
gi 239938634   166 LHNLLRCVERAGIEITDICLQPLAAGSAA 194
Cdd:smart00842 159 IQNLEKCVERAGLEVDGIVLEPLASAEAV 187
FtsA pfam14450
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
 205-366 3.57e-53

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.


Pssm-ID: 464177 [Multi-domain]  Cd Length: 167  Bit Score: 175.60  E-value: 3.57e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  205 ALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIGLRTSTEEAERVKKQLGHAYYDEASEDeifEVTVIGTNQKQ 284
Cdd:pfam14450   1 ALIDIGGGTTDIAVFEDGALRHTRVIPVGGNGITKDIAIGLRTAVEEAERLKIKYGSALASLADED---EVPGVGGREPR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  285 TFTQQEAANIIEARVEEILEIVSEELRSMG--------ITDLPGGFVLTGGQAAMPGVMSLAQDVLQNNVRVASPNYIGV 356
Cdd:pfam14450  78 EISRKELAEIIEARVEEILELVRAELEDREvlpgeyvrLEVDVHGIVLTGGGSALPGLVELAERALGLPVRIGSPDGIGG 157

                         170
                  ....*....|
gi 239938634  357 RDPQYMTGVG 366
Cdd:pfam14450 158 RNPAYATALG 167
ASKHA_NBD_PilM-like cd24004
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ...
 8-368 1.19e-40

nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466854 [Multi-domain]  Cd Length: 282  Bit Score: 146.28  E-value: 1.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   8 VSLDIGTSNTKVIVGEMTDDSLNIIGVGNVPSEGL--KKGSIVDIDETVHSIRKAFDQAERMVGFPLRKAIVGvngnyin 85
Cdd:cd24004    1 FALDIGTRSIKGLVLEEDDENIEVLAFSSEEHPERamGDGQIHDISKVAESIKELLKELEEKLGSKLKDVVIA------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  86 iqdtngvvavssenkeiqvedvrrvmeaaqvvsvpheqlivdvIPKqfIVDGrdeitdpkkmlgvrlevegtlitgskti 165
Cdd:cd24004   74 -------------------------------------------IAK--VVES---------------------------- 80

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 166 lhnLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIGL 245
Cdd:cd24004   81 ---LLNVLEKAGLEPVGLTLEPFAAANLLIPYDMRDLNIALVDIGAGTTDIALIRNGGIEAYRMVPLGGDDFTKAIAEGF 157

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 246 RTSTEEAERVKKQLGHAYYDEASEDEIFEVTVIgtnqkqtftqqEAANIIEARVEEILEIVSEELRSM-GITDLPGGFVL 324
Cdd:cd24004  158 LISFEEAEKIKRTYGIFLLIEAKDQLGFTINKK-----------EVYDIIKPVLEELASGIANAIEEYnGKFKLPDAVYL 226

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 239938634 325 TGGQAAMPGVMSLAQDVLQNNV-RVASPNYIGV----------RDPQYMTGVGLI 368
Cdd:cd24004  227 VGGGSKLPGLNEALAEKLGLPVeRIAPRNIGAIsditdetskaKGPEFVTPLGIA 281
ASKHA_NBD_PilM cd24049
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ...
 8-351 8.76e-33

nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.


Pssm-ID: 466899 [Multi-domain]  Cd Length: 339  Bit Score: 126.62  E-value: 8.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   8 VSLDIGTSNTKVIVGEMTDDSLNIIGVG--NVPSEGLKKGSIVDIDETVHSIRKAFDQAermvGFPLRKAIVGVNGNYIN 85
Cdd:cd24049    1 LGIDIGSSSIKAVELKRSGGGLVLVAFAiiPLPEGAIVDGEIADPEALAEALKKLLKEN----KIKGKKVVVALPGSDVI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  86 IQDTNgvVAVSSEnKEIQvEDVRrvMEAAQVVSVPHEQLIVDvipkqFIVDGRDEITDPKkmlgvrleVEGTLITGSKTI 165
Cdd:cd24049   77 VRTIK--LPKMPE-KELE-EAIR--FEAEQYLPFPLEEVVLD-----YQILGEVEEGGEK--------LEVLVVAAPKEI 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 166 LHNLLRCVERAGIEITDICLQPLAAGSA--ALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISI 243
Cdd:cd24049  138 VESYLELLKEAGLKPVAIDVESFALARAleYLLPDEEEETVALLDIGASSTTLVIVKNGKLLFTRSIPVGGNDITEAIAK 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 244 GLRTSTEEAERVKKQLGHAYYDEASEDEIFEVTVigtnqkqtftqQEAANIIEARVEEILEIVSEELRSMGITDLpggfV 323
Cdd:cd24049  218 ALGLSFEEAEELKREYGLLLEGEEGELKKVAEAL-----------RPVLERLVSEIRRSLDYYRSQNGGEPIDKI----Y 282

                        330       340
                 ....*....|....*....|....*...
gi 239938634 324 LTGGQAAMPGVMSLAQDVLQNNVRVASP 351
Cdd:cd24049  283 LTGGGSLLPGLDEYLSERLGIPVEILNP 310
SHS2_FTSA pfam02491
SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes ...
 87-160 7.30e-21

SHS2 domain inserted in FTSA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. The SHS2 domain is inserted in to the RNAseH fold of FtsA, and is involved in protein-protein interaction.


Pssm-ID: 460571 [Multi-domain]  Cd Length: 73  Bit Score: 86.01  E-value: 7.30e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239938634   87 QDTNGVVAVSseNKEIQVEDVRRVMEAAQVVSVPHEQLIVDVIPKQFIVDGRDEITDPKKMLGVRLEVEGTLIT 160
Cdd:pfam02491   2 QNSSGVVAIS--GREITEEDVDRVLEAARAVAIPPDREILHVLPQEFIVDGQEGIKDPVGMSGVRLEADVHVVT 73
PilM COG4972
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures];
7-233 1.86e-17

Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures];


Pssm-ID: 443997 [Multi-domain]  Cd Length: 294  Bit Score: 82.21  E-value: 1.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   7 YVSLDIGTSNTKVIVGEMTDDSLNIIGVG--NVPSEGLKKGSIVDIDETVHSIRKAFDQAermvGFPLRKAIVGVNGNYI 84
Cdd:COG4972    4 LVGIDIGSSSIKLVELSKSGGGYRLERYAeePLPEGAVVDGNIVDPEAVAEALKELLKRL----KIKTKRVAIAVPGSSV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  85 NIQDTNgVVAVSSENKEIQVEdvrrvMEAAQVVSVPHEQLIVDvipkqFIVDGRDEiTDPKKMlgvrlEVegtLITGS-K 163
Cdd:COG4972   80 ITRKIT-LPALSEKELEEAIE-----FEAEQYIPFPLEEVVLD-----FQVLGPSE-EGPEKV-----EV---LLVAArK 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 239938634 164 TILHNLLRCVERAGIEITDICLQPLAAGSAA--LSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLG 233
Cdd:COG4972  140 EVVEDYVELLEAAGLKPVVVDVEPFALLRALelLPPSGPDETVALVDIGASSTTLSVLSNGKPIFTREIPFG 211
ASKHA_NBD_MreB-like cd10225
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ...
 173-349 2.20e-15

nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466824 [Multi-domain]  Cd Length: 317  Bit Score: 76.74  E-value: 2.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 173 VERAGIeiTDICL--QPLAAGSAA-LSKDEKNlGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDIS------- 242
Cdd:cd10225  114 AEHAGA--REVYLieEPMAAAIGAgLPIEEPR-GSMVVDIGGGTTEIAVISLGGIVTSRSVRVAGDEMDEAIInyvrrky 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 243 ---IGLRTsteeAERVKKQLGHAYYDEasEDEIFEVT----VIGTNQKQTFTQQEAANIIEARVEEILEIVSEELRSM-- 313
Cdd:cd10225  191 nllIGERT----AERIKIEIGSAYPLD--EELSMEVRgrdlVTGLPRTIEITSEEVREALEEPVNAIVEAVRSTLERTpp 264

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 239938634 314 ----GITDlpGGFVLTGGQAAMPGVMSLAQDVLQNNVRVA 349
Cdd:cd10225  265 elaaDIVD--RGIVLTGGGALLRGLDELLREETGLPVHVA 302
ASKHA_NBD_EutJ cd24047
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ...
 92-367 6.57e-15

nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.


Pssm-ID: 466897 [Multi-domain]  Cd Length: 241  Bit Score: 73.84  E-value: 6.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  92 VVAVSSENKEIQVEdvrrvMEAAQVVsvpHEQLIVDVIPKQFIVdgRDEITDPKKMLGVRLEVE------GTLITGSKTI 165
Cdd:cd24047   14 LVVVDEEGQPVAGA-----LERADVV---RDGIVVDYIGAIRIV--RKLKETLEKKLGVELTSAatafppGTGERDARAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 166 LHnllrCVERAGIEITDICLQPLAAGSAalskdeknLGV---ALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDIS 242
Cdd:cd24047   84 RN----VLEGAGLEVSNVVDEPTAANAV--------LGIrdgAVVDIGGGTTGIAVLKDGKVVYTADEPTGGTHLSLVLA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 243 IGLRTSTEEAERVKKqlghayyDEASEDEIFEvtvigtnqkqtftqqeaanIIEARVEEILEIVSEELRSMGITDLpggf 322
Cdd:cd24047  152 GNYGISFEEAEIIKR-------DPARHKELLP-------------------VVRPVIEKMASIVKRHIKGYKVKDL---- 201

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 239938634 323 VLTGGQAAMPGVMSLAQDVLQNNVRVASpnyigvrDPQYMTGVGL 367
Cdd:cd24047  202 YLVGGTCCLPGIEEVFEKETGLPVYKPS-------NPLLVTPLGI 239
PRK13930 PRK13930
rod shape-determining protein MreB; Provisional
 207-349 1.48e-11

rod shape-determining protein MreB; Provisional


Pssm-ID: 237564 [Multi-domain]  Cd Length: 335  Bit Score: 65.15  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 207 IDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDI----------SIGLRTsteeAERVKKQLGHAYYDEasEDEIFEVT 276
Cdd:PRK13930 157 VDIGGGTTEVAVISLGGIVYSESIRVAGDEMDEAIvqyvrrkynlLIGERT----AEEIKIEIGSAYPLD--EEESMEVR 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 277 ----VIGTNQKQTFTQQEAANIIEARVEEILEIVSEELR------SMGITDlpGGFVLTGGQAAMPGVMSLAQDVLQNNV 346
Cdd:PRK13930 231 grdlVTGLPKTIEISSEEVREALAEPLQQIVEAVKSVLEktppelAADIID--RGIVLTGGGALLRGLDKLLSEETGLPV 308


                 ...
gi 239938634 347 RVA 349
Cdd:PRK13930 309 HIA 311
pilM TIGR01175
type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV ...
 8-367 8.66e-11

type IV pilus assembly protein PilM; This protein is required for the assembly of the type IV fimbria in Pseudomonas aeruginosa responsible for twitching motility, and for a similar pilus-like structure in Synechocystis. It is also found in species such as Deinococcus described as having natural transformation (for which a type IV pilus-like structure is proposed) but not fimbria.


Pssm-ID: 273484 [Multi-domain]  Cd Length: 348  Bit Score: 62.88  E-value: 8.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634    8 VSLDIGTSNTKVIVGEMTDDSLNIIGVGN--VPSEGLKKGSIVDIDETVHSIRKAFDQAermvGFPLRKAIVGVNGNYIN 85
Cdd:TIGR01175   6 VGIDIGSTSVKVAQLKRSGDRYKLEHYAVepLPAGIFTEGHIVEYQAVAEALKELLSEL----GINTKKAATAVPGSAVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   86 IQdtngVVAVSSENKEIQVEDVRRVmEAAQVVSVPHEQLIVDVipkqfivdgrDEITDPKKMLGVRLEVegtLITGSKT- 164
Cdd:TIGR01175  82 TK----VIPVPAGLDERELEFAVYI-EASHYIPYPIEEVSLDF----------EKLGLKANNPESTVQV---LLAATRKe 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  165 ILHNLLRCVERAGIEITDICLQPLAA------GSAALSKDEKNL-GVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENI 237
Cdd:TIGR01175 144 VVDSRLHALKLAGLEPKVVDVESFALlrawrlLGEQLASRTYRLtDAALVDIGATSSTLNLLHPGRMLFTREVPFGTRQL 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  238 TKDISIGLRTSTEEAERVKKQLGHAyydeasedEIFEVTVIGTnQKQTFTQQEAANIiearveEILEIVSEELRSmgitd 317
Cdd:TIGR01175 224 TSELSRAYGLNPEEAGEAKQQGGLP--------LLYDPEVLRR-FKGELVDEIRRSL------QFFTAQSGTNSL----- 283

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 239938634  318 lpGGFVLTGGQAAMPGVMSLAQDVLQNNVRVASP------------NYIGVRDPQYMTGVGL 367
Cdd:TIGR01175 284 --DGLVLAGGGATLSGLDAAIYQRLGLPTEVANPfalmaldakvdaGRLAVDAPALMTALGL 343
MreB COG1077
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ...
 207-349 9.49e-11

Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 440695 [Multi-domain]  Cd Length: 339  Bit Score: 62.79  E-value: 9.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 207 IDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDI----------SIGLRTsteeAERVKKQLGHAYYDEasEDEIFEVT 276
Cdd:COG1077  156 VDIGGGTTEVAVISLGGIVVSRSIRVAGDELDEAIiqyvrkkynlLIGERT----AEEIKIEIGSAYPLE--EELTMEVR 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 277 ----VIGTNQKQTFTQQEAANIIEARVEEILEIVSE-------ELRSmGITDlpGGFVLTGGQAAMPGVMSLAQDVLQNN 345
Cdd:COG1077  230 grdlVTGLPKTITITSEEIREALEEPLNAIVEAIKSvlektppELAA-DIVD--RGIVLTGGGALLRGLDKLLSEETGLP 306


                 ....
gi 239938634 346 VRVA 349
Cdd:COG1077  307 VHVA 310
PRK15080 PRK15080
ethanolamine utilization protein EutJ; Provisional
 92-372 4.31e-10

ethanolamine utilization protein EutJ; Provisional


Pssm-ID: 237904 [Multi-domain]  Cd Length: 267  Bit Score: 60.23  E-value: 4.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  92 VVAVSSENKEIqvedVRRVMEAAQVVsvpHEQLIVDVIPKQFIVdgRDEITDPKKMLGVRLEVEGTLI-----TGSKTIL 166
Cdd:PRK15080  37 VLAVLDEDGQP----VAGALEWADVV---RDGIVVDFIGAVTIV--RRLKATLEEKLGRELTHAATAIppgtsEGDPRAI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 167 HNLlrcVERAGIEITDICLQPLAAGSAalskdeknLGV---ALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISI 243
Cdd:PRK15080 108 INV---VESAGLEVTHVLDEPTAAAAV--------LGIdngAVVDIGGGTTGISILKDGKVVYSADEPTGGTHMSLVLAG 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 244 GLRTSTEEAERVKKqlghayyDEASEDEIFEVtvigtnqkqtftqqeaaniIEARVEEILEIVSEELRSMGITDLpggfV 323
Cdd:PRK15080 177 AYGISFEEAEQYKR-------DPKHHKEIFPV-------------------VKPVVEKMASIVARHIEGQDVEDI----Y 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 239938634 324 LTGGQAAMPGVMSLAQDVLQnnVRVASPNYigvrdPQYMTGVGlIQFAC 372
Cdd:PRK15080 227 LVGGTCCLPGFEEVFEKQTG--LPVHKPQH-----PLFVTPLG-IALSC 267
PilM_2 pfam11104
Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for ...
 10-257 5.21e-10

Type IV pilus assembly protein PilM;; The type IV pilus assembly protein PilM is required for competency and pilus biogenesis. It binds to PilN and ATP.


Pssm-ID: 431656 [Multi-domain]  Cd Length: 340  Bit Score: 60.77  E-value: 5.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   10 LDIGTSNTKVIVGEMTDDSLNI--IGVGNVPSEGLKKGSIVDIDETVHSIRKAFDQAermvGFPLRKAIVGVNGNYINIQ 87
Cdd:pfam11104   2 IDISSSAIKLVELSKKKGGYRLerYAIEPLPKGAVVDGNIENIDAVSEALRRAVKKS----GTRLKNVAIAVPGSAVITK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   88 DTNGVVAVSSENKEIQVEdvrrvMEAAQVVSVPHEQLIVDvipkqFIVDGRDeITDPKKMlgvrlEVegtLITGSKT-IL 166
Cdd:pfam11104  78 KIILPAGLSEEELEAQVE-----IEANQYIPFPLDEVSLD-----FEVLGPN-AANPDDV-----DV---LLAAARKeKV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  167 HNLLRCVERAGI--EITDICLQPLAAGSA----ALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKD 240
Cdd:pfam11104 139 EDRVDLLEAAGLkpKVVDVESYALERAFErivsQLPNDGKDKCVAIVDIGANMTTLSVLRNGEIIYTREQAFGGAQLTQE 218

                         250
                  ....*....|....*..
gi 239938634  241 ISIGLRTSTEEAERVKK 257
Cdd:pfam11104 219 IVRRYGMSYEEAEIAKR 235
MreB_Mbl pfam06723
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ...
 207-349 5.17e-09

MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.


Pssm-ID: 399596 [Multi-domain]  Cd Length: 327  Bit Score: 57.57  E-value: 5.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  207 IDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDI----------SIGLRTsteeAERVKKQLGHAYYDEasEDEIFEV- 275
Cdd:pfam06723 150 VDIGGGTTEVAVISLGGIVTSKSVRVAGDEFDEAIikyirkkynlLIGERT----AERIKIEIGSAYPTE--EEEKMEIr 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634  276 ---TVIGTNQKQTFTQQEAANIIEARVEEILEIVSEELR------SMGITDlpGGFVLTGGQAAMPGVMSLAQDVLQNNV 346
Cdd:pfam06723 224 grdLVTGLPKTIEISSEEVREALKEPVSAIVEAVKEVLEktppelAADIVD--RGIVLTGGGALLRGLDKLLSDETGLPV 301


                  ...
gi 239938634  347 RVA 349
Cdd:pfam06723 302 HIA 304
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
 169-348 3.20e-08

nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466811 [Multi-domain]  Cd Length: 329  Bit Score: 55.19  E-value: 3.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 169 LLRCVERAGIEITDICLQ----PLAAGSAAL------SKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRV--------I 230
Cdd:cd10170   93 LREAARAAGFGSDSDNVRlvsePEAAALYALedkgdlLPLKPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLeevapgggA 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 231 PLGGENIT-------------------KDISIGLRTSTEEAERVKKQL---GHAYYDEASEDEIFEVTVIGTNQKQTFTQ 288
Cdd:cd10170  173 LLGGTDIDeafekllreklgdkgkdlgRSDADALAKLLREFEEAKKRFsggEEDERLVPSLLGGGLPELGLEKGTLLLTE 252

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 289 QEAANIIEARVEEILEIVSEELRSMGITDlPGGFVLTGGQAAMPGVMSLAQDVLQNNVRV 348
Cdd:cd10170  253 EEIRDLFDPVIDKILELIEEQLEAKSGTP-PDAVVLVGGFSRSPYLRERLRERFGSAGII 311
PRK13927 PRK13927
rod shape-determining protein MreB; Provisional
 203-329 1.07e-07

rod shape-determining protein MreB; Provisional


Pssm-ID: 237562 [Multi-domain]  Cd Length: 334  Bit Score: 53.55  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 203 GVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDIS----------IGLRTsteeAERVKKQLGHAYydeaSEDEI 272
Cdd:PRK13927 149 GSMVVDIGGGTTEVAVISLGGIVYSKSVRVGGDKFDEAIInyvrrnynllIGERT----AERIKIEIGSAY----PGDEV 220

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239938634 273 FEVTVIGTNQ------KQTFTQQEAA--------NIIEArVEEILEIVSEELrSMGITDLpgGFVLTGGQA 329
Cdd:PRK13927 221 LEMEVRGRDLvtglpkTITISSNEIRealqeplsAIVEA-VKVALEQTPPEL-AADIVDR--GIVLTGGGA 287
PRK13928 PRK13928
rod shape-determining protein Mbl; Provisional
 186-349 2.31e-07

rod shape-determining protein Mbl; Provisional


Pssm-ID: 237563 [Multi-domain]  Cd Length: 336  Bit Score: 52.21  E-value: 2.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 186 QPLAAGSAALSKDEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDIS----------IGLRTsteeAERV 255
Cdd:PRK13928 131 EPLAAAIGAGLDISQPSGNMVVDIGGGTTDIAVLSLGGIVTSSSIKVAGDKFDEAIIryirkkykllIGERT----AEEI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 256 KKQLGHAYYDeaSEDEIFEVT----VIGTNQKQTFTQQEAANIIEARVEEILEIVSEELR------SMGITDlpGGFVLT 325
Cdd:PRK13928 207 KIKIGTAFPG--AREEEMEIRgrdlVTGLPKTITVTSEEIREALKEPVSAIVQAVKSVLErtppelSADIID--RGIIMT 282

                        170       180
                 ....*....|....*....|....
gi 239938634 326 GGQAAMPGVMSLAQDVLQNNVRVA 349
Cdd:PRK13928 283 GGGALLHGLDKLLAEETKVPVYIA 306
FtsA pfam14450
Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to ...
 10-176 3.51e-07

Cell division protein FtsA; FtsA is essential for bacterial cell division, and co-localizes to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491.


Pssm-ID: 464177 [Multi-domain]  Cd Length: 167  Bit Score: 50.02  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   10 LDIGTSNTKVIVGEmtDDSL---NIIGVGnvpSEGLKKGsivdideTVHSIRKAFDQAERMVGFPLRKAIVGVNGNYINI 86
Cdd:pfam14450   3 IDIGGGTTDIAVFE--DGALrhtRVIPVG---GNGITKD-------IAIGLRTAVEEAERLKIKYGSALASLADEDEVPG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634   87 QDTNGVVAVSSEN-KEIQVEDVRRVMEAAQvvsvpheqlivdvipkqFIVDGRDEITDPKKMLGVrlEVEGTLITGSKTI 165
Cdd:pfam14450  71 VGGREPREISRKElAEIIEARVEEILELVR-----------------AELEDREVLPGEYVRLEV--DVHGIVLTGGGSA 131

                         170
                  ....*....|.
gi 239938634  166 LHNLLRCVERA 176
Cdd:pfam14450 132 LPGLVELAERA 142
PRK13929 PRK13929
rod-share determining protein MreBH; Provisional
 169-348 3.68e-06

rod-share determining protein MreBH; Provisional


Pssm-ID: 184403 [Multi-domain]  Cd Length: 335  Bit Score: 48.75  E-value: 3.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 169 LLRCVERAGIEITDICLQPLAAG-SAALSKDEKNLGVaLIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDIS----- 242
Cdd:PRK13929 117 ISDAVKNCGAKNVHLIEEPVAAAiGADLPVDEPVANV-VVDIGGGTTEVAIISFGGVVSCHSIRIGGDQLDEDIVsfvrk 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 243 -----IGLRTsteeAERVKKQLGHAYYDEasEDEIFEVT----VIGTNQKQTFTQQEAANIIEARVEEILEIVSEELR-- 311
Cdd:PRK13929 196 kynllIGERT----AEQVKMEIGYALIEH--EPETMEVRgrdlVTGLPKTITLESKEIQGAMRESLLHILEAIRATLEdc 269

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 239938634 312 ----SMGITDLpgGFVLTGGQAAMPGVmslaQDVLQNNVRV 348
Cdd:PRK13929 270 ppelSGDIVDR--GVILTGGGALLNGI----KEWLSEEIVV 304
DnaK COG0443
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ...
 174-334 3.73e-06

Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440212 [Multi-domain]  Cd Length: 473  Bit Score: 49.05  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 174 ERAGIEITDICLQPLAA----GSAALSKDEKnlgVALIDIGGGSTTIAV--FQNGH---LTSTRVIPLGGENIT------ 238
Cdd:COG0443  135 RIAGLEVLRLLNEPTAAalayGLDKGKEEET---ILVYDLGGGTFDVSIlrLGDGVfevLATGGDTHLGGDDFDqalady 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 239 ------KDISIGLRTS-------TEEAERVKKQLghayydeaSEDEIFEVTV---IGTNQKQTFTQQEAANIIEARVEEI 302
Cdd:COG0443  212 vapefgKEEGIDLRLDpaalqrlREAAEKAKIEL--------SSADEAEINLpfsGGKHLDVELTRAEFEELIAPLVERT 283

                        170       180       190
                 ....*....|....*....|....*....|...
gi 239938634 303 LEIVSEELRSMGIT-DLPGGFVLTGGQAAMPGV 334
Cdd:COG0443  284 LDPVRQALADAGLSpSDIDAVLLVGGSTRMPAV 316
eutA PRK10719
ethanolamine ammonia-lyase reactivating factor EutA;
190-234 1.34e-05

ethanolamine ammonia-lyase reactivating factor EutA;


Pssm-ID: 236743 [Multi-domain]  Cd Length: 475  Bit Score: 47.17  E-value: 1.34e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 239938634 190 AGSAALSKdEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGG 234
Cdd:PRK10719 135 AGAQTLSE-ERNTRVLNIDIGGGTANYALFDAGKVIDTACLNVGG 178
EutA pfam06277
Ethanolamine utilization protein EutA; This family consists of several bacterial EutA ...
 190-234 2.32e-05

Ethanolamine utilization protein EutA; This family consists of several bacterial EutA ethanolamine utilization proteins. The EutA protein is thought to protect the lyase (EutBC) from inhibition by CNB12.


Pssm-ID: 377642  Cd Length: 475  Bit Score: 46.47  E-value: 2.32e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 239938634  190 AGSAALSKdEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGG 234
Cdd:pfam06277 132 AGAAAYSK-EHHTRVLNIDIGGGTSNIALFKAGEVIDTACLDVGG 175
ASKHA_NBD_PPX_GppA cd24006
nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate ...
 198-313 8.23e-05

nucleotide-binding domain (NBD) of the exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GppA) domain family; Members of the PPX/GppA family are involved in bacterial survival and metabolism. They may play distinct biochemical roles involved in polyphosphate and (p)ppGpp metabolic pathways. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). Some bacteria, such as Escherichia coli, possesses two homologs, EcGppA and EcPPX. Some others, such as Helicobacter pylori and Aquifex aeolicus, encode only one PPX/GppA homolog, which may play important roles in the homeostasis of both (p)ppGpp and PolyP. The PPX/GppA family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466856 [Multi-domain]  Cd Length: 294  Bit Score: 44.06  E-value: 8.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 198 DEKNLGVALIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIGLRTSTEEAERVKKQLGHAYYDEASEDEIFEVTV 277
Cdd:cd24006  122 PLGDGNALIVDIGGGSTELTLGDNGEILFSESLPLGAVRLTERFLKDDPPSELLEEYLRSFVRSVLRPLPKRRKIKFDVA 201

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 239938634 278 IGTN------QKQTFTQQEAANIIEARVEEILEIVsEELRSM 313
Cdd:cd24006  202 IGSGgtilalAAMALARKGKPHGYEISREELKALY-DELLRL 242
ASKHA_NBD_HpPPX-GppA-like cd24052
nucleotide-binding domain (NBD) of Helicobacter pylori exopolyphosphatase/guanosine ...
 206-257 1.26e-04

nucleotide-binding domain (NBD) of Helicobacter pylori exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (HpPPX/GppA) and similar proteins; The PPX/GppA family proteins play essential roles in bacterial survival and metabolism. Guanosine pentaphosphate (pppGpp) phosphohydrolase (GppA; EC 3.6.1.40) plays a key role in (p)ppGpp homeostasis. It specifically catalyzes the conversion of pppGpp to ppGpp (guanosine tetraphosphate). Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX; EC 3.6.1.11), which mediates the metabolism of cellular inorganic polyphosphate. Especially, it is responsible for the maintenance of appropriate levels of cellular inorganic polyphosphate (PolyP). The family corresponds a group of proteins similar to Helicobacter pylori PPX/GppA (HpPPX/GppA). HpPPX/GppA is phylogenetically distant from the Escherichia coli homologs. Unlike E. coli that possesses two homologs, EcGppA and EcPPX, H. pylori encodes only one PPX/GppA homolog, HpPPX/GppA. As such, HpPPX/GppA may play important roles in the homeostasis of both (p)ppGpp and PolyP.


Pssm-ID: 466902 [Multi-domain]  Cd Length: 298  Bit Score: 43.62  E-value: 1.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 239938634 206 LIDIGGGSTTIAVFQNGHLTSTRVIPLGGENITKDISIGLRTSTEEAERVKK 257
Cdd:cd24052  128 VVDIGGGSTELVLFKNGKIKESISLPLGSLRLYERFVSGILPTEKELKKIRK 179
ASKHA_NBD_HSP70_HscA cd10236
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ...
 176-334 3.02e-04

nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar proteins; Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HscA's partner J-domain protein is HscB; it does not appear to require a NEF and has been shown to be induced by cold-shock. The HscA-HscB chaperone/co-chaperone pair is involved in [Fe-S] cluster assembly.


Pssm-ID: 466834 [Multi-domain]  Cd Length: 367  Bit Score: 42.59  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 176 AGIEITDICLQPLAAgSAALSKDEKNLGV-ALIDIGGGSTTIA-------VFQ----NGHLTstrvipLGG--------E 235
Cdd:cd10236  159 AGLNVLRLLNEPTAA-ALAYGLDQKKEGTiAVYDLGGGTFDISilrlsdgVFEvlatGGDTA------LGGddfdhllaD 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 236 NITKDISIGLRTSTEE-------AERVKKQLghAYYDEASEdeifEVTVIGTNQKQTFTQQEAANIIEARVEEILEIVSE 308
Cdd:cd10236  232 WILKQIGIDARLDPAVqqallqaARRAKEAL--SDADSASI----EVEVEGKDWEREITREEFEELIQPLVKRTLEPCRR 305

                        170       180
                 ....*....|....*....|....*..
gi 239938634 309 ELRSMGIT-DLPGGFVLTGGQAAMPGV 334
Cdd:cd10236  306 ALKDAGLEpADIDEVVLVGGSTRIPLV 332
ASKHA_NBD_HSP70_DnaK_HscA_HscC cd24029
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ...
 174-344 4.92e-04

nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and similar proteins; Escherichia coli DnaK, also called heat shock 70 kDa protein/HSP70, plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Moreover, DnaK participates actively in the response to hyperosmotic shock. Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. The family also includes Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.


Pssm-ID: 466879 [Multi-domain]  Cd Length: 351  Bit Score: 42.18  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 174 ERAGIEITDICLQPLAA----GSAALSKDEKnlgVALIDIGGGSTTIAVF--QNGHLtstRVIP------LGGENITK-- 239
Cdd:cd24029  134 ELAGLNVLRLINEPTAAalayGLDKEGKDGT---ILVYDLGGGTFDVSILeiENGKF---EVLAtggdnfLGGDDFDEai 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 240 --------DISIGLRTSTE----------EAERVKKQLGHAYydeaSEDEIFEVTVIGTNQKQTFTQQEAANIIEARVEE 301
Cdd:cd24029  208 aelilekiGIETGILDDKEderararlreAAEEAKIELSSSD----STDILILDDGKGGELEIEITREEFEELIAPLIER 283

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 239938634 302 ILEIVSEELRSMGIT-DLPGGFVLTGGQAAMPGVMSLAQDVLQN 344
Cdd:cd24029  284 TIDLLEKALKDAKLSpEDIDRVLLVGGSSRIPLVREMLEEYFGR 327
ASKHA_NBD_ParM-like cd10227
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ...
 153-239 2.83e-03

nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466825 [Multi-domain]  Cd Length: 263  Bit Score: 39.43  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938634 153 EVEGTLITGSKTILHNLLRCVERAGIEITDICLQPLAAGSAALSKDEKNLG----VALIDIGGGSTTIAVFQNG--HLTS 226
Cdd:cd10227  110 EEKKELKKKLLKGLHEFTFNGKERRITINDVKVLPEGAGAYLDYLLDDDELedgnVLVIDIGGGTTDILTFENGkpIEES 189

                         90
                 ....*....|...
gi 239938634 227 TRVIPLGGENITK 239
Cdd:cd10227  190 SDTLPGGEEALEK 202
ASKHA_NBD_FGGY_RhaB-like cd07771
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ...
 7-65 9.92e-03

nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.


Pssm-ID: 466791 [Multi-domain]  Cd Length: 460  Bit Score: 38.28  E-value: 9.92e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239938634   7 YVSLDIGTSNTKVIVGEMTDDSLNIIGVGNVPSEGLKKGSIV--DID----ETVHSIRKAFDQAE 65
Cdd:cd07771    2 YLAVDLGASSGRVILGSLDGGKLELEEIHRFPNRPVEINGHLywDIDrlfdEIKEGLKKAAEQGG 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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