|
Name |
Accession |
Description |
Interval |
E-value |
| MurT_C |
pfam08353 |
MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from ... |
319-429 |
5.93e-44 |
|
MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from Gram-positive bacteria. MurT is part of the bi-enzymatic complex MurT-GatD involved in the amidation of the alpha-carboxyl group of the D-isoglutamate residue in Lipid II in the peptidoglycan layer to produce D-isoglutamine. This domain contains an aspartate at position 349, the third residue in the catalytic triad GatD-C94, GatD-H189, MurT-D349. This C-terminal domain is built around a central six-stranded, predominantly parallel beta-sheet that is sandwiched between four alpha-helices on one side and two alpha-helices on the other. The MurT-GatD heterodimer adopts a boomerang-shaped conformation, with GatD packing against the C-terminal domain of MurT. :
Pssm-ID: 462442 Cd Length: 110 Bit Score: 149.56 E-value: 5.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 319 LIKNPVGASQALEMIQLADYPFSLSVLLNANYADGIDTSWIWDANFELITHMPITEINAGGVRHSEIARRLRVTGFDDTK 398
Cdd:pfam08353 1 LVKNPVGFNQVLNYIASDPGPKSLLLLLNDNYADGRDVSWIWDVDFEKLNDSNIKKIIVSGDRAYDMALRLKYAGVPEEK 80
|
90 100 110
....*....|....*....|....*....|.
gi 407968025 399 IKQAEKLEQITEAIeKQESKHAYILATYTAM 429
Cdd:pfam08353 81 IEIEEDLEEALDAI-KAPTENVYILPTYTAM 110
|
|
| MurC super family |
cl34041 |
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ... |
39-294 |
3.01e-15 |
|
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis The actual alignment was detected with superfamily member COG0773:
Pssm-ID: 440536 [Multi-domain] Cd Length: 451 Bit Score: 77.41 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 39 DILDSLSKDYEIVVITGTNGKTLTTALTVGILKEAfgdvltnpsGAN---MITGITAAF-LSAKKGKSgkHIAVLEIDE- 113
Cdd:COG0773 95 EMLAELMRGKRSIAVAGTHGKTTTTSMLAHILEEA---------GLDptfLIGGILNNFgTNARLGDG--DYFVAEADEs 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 114 -ASLpkitNYLKPSLFVYTNIFRDQMDrygeIYTTYQMIVDG----ARNAPKA-TILANGDSPIfsSKDIV----NPVQY 183
Cdd:COG0773 164 dGSF----LHYSPDIAVVTNIEADHLD----IYGDLEAIKEAfhefARNVPFYgLLVLCADDPG--LRELLprcgRPVIT 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 184 YGFDtakhapqlahyntegilcpkcehilqyrlntyanlgdficlncqfqrPTLDYQLTELTAITHQSS-EFVIDGQNY- 261
Cdd:COG0773 234 YGFS-----------------------------------------------EDADYRAENIRIDGGGSTfDVLRRGEELg 266
|
250 260 270
....*....|....*....|....*....|....*
gi 407968025 262 --KINVGGLYNIYNALAAVSVAEFFGVSPEKIKAG 294
Cdd:COG0773 267 evELNLPGRHNVLNALAAIAVALELGVDPEAIAEA 301
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MurT_C |
pfam08353 |
MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from ... |
319-429 |
5.93e-44 |
|
MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from Gram-positive bacteria. MurT is part of the bi-enzymatic complex MurT-GatD involved in the amidation of the alpha-carboxyl group of the D-isoglutamate residue in Lipid II in the peptidoglycan layer to produce D-isoglutamine. This domain contains an aspartate at position 349, the third residue in the catalytic triad GatD-C94, GatD-H189, MurT-D349. This C-terminal domain is built around a central six-stranded, predominantly parallel beta-sheet that is sandwiched between four alpha-helices on one side and two alpha-helices on the other. The MurT-GatD heterodimer adopts a boomerang-shaped conformation, with GatD packing against the C-terminal domain of MurT.
Pssm-ID: 462442 Cd Length: 110 Bit Score: 149.56 E-value: 5.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 319 LIKNPVGASQALEMIQLADYPFSLSVLLNANYADGIDTSWIWDANFELITHMPITEINAGGVRHSEIARRLRVTGFDDTK 398
Cdd:pfam08353 1 LVKNPVGFNQVLNYIASDPGPKSLLLLLNDNYADGRDVSWIWDVDFEKLNDSNIKKIIVSGDRAYDMALRLKYAGVPEEK 80
|
90 100 110
....*....|....*....|....*....|.
gi 407968025 399 IKQAEKLEQITEAIeKQESKHAYILATYTAM 429
Cdd:pfam08353 81 IEIEEDLEEALDAI-KAPTENVYILPTYTAM 110
|
|
| MurC |
COG0773 |
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ... |
39-294 |
3.01e-15 |
|
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440536 [Multi-domain] Cd Length: 451 Bit Score: 77.41 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 39 DILDSLSKDYEIVVITGTNGKTLTTALTVGILKEAfgdvltnpsGAN---MITGITAAF-LSAKKGKSgkHIAVLEIDE- 113
Cdd:COG0773 95 EMLAELMRGKRSIAVAGTHGKTTTTSMLAHILEEA---------GLDptfLIGGILNNFgTNARLGDG--DYFVAEADEs 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 114 -ASLpkitNYLKPSLFVYTNIFRDQMDrygeIYTTYQMIVDG----ARNAPKA-TILANGDSPIfsSKDIV----NPVQY 183
Cdd:COG0773 164 dGSF----LHYSPDIAVVTNIEADHLD----IYGDLEAIKEAfhefARNVPFYgLLVLCADDPG--LRELLprcgRPVIT 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 184 YGFDtakhapqlahyntegilcpkcehilqyrlntyanlgdficlncqfqrPTLDYQLTELTAITHQSS-EFVIDGQNY- 261
Cdd:COG0773 234 YGFS-----------------------------------------------EDADYRAENIRIDGGGSTfDVLRRGEELg 266
|
250 260 270
....*....|....*....|....*....|....*
gi 407968025 262 --KINVGGLYNIYNALAAVSVAEFFGVSPEKIKAG 294
Cdd:COG0773 267 evELNLPGRHNVLNALAAIAVALELGVDPEAIAEA 301
|
|
| murD |
TIGR01087 |
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ... |
17-309 |
2.52e-14 |
|
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273436 [Multi-domain] Cd Length: 433 Bit Score: 74.68 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 17 LILKKLGRGSTYPGRLALAFDKDildslskDYEIVVITGTNGKTLTTALTVGILKEAFGDVltnPSGANmitgITAAFLS 96
Cdd:TIGR01087 78 LVQAAAKRGIPVVGDIELFLRLV-------PLPVVAITGTNGKTTTTSLLYHLLKAAGLKA---FLGGN----IGTPALE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 97 AKKGKsGKHIAVLEIDEASLpKITNYLKPSLFVYTNIFRDQMDRYG--EIYT-TYQMIVDGARNApkATILANGDSPIFS 173
Cdd:TIGR01087 144 VLDQE-GAELYVLELSSFQL-ETTESLRPEIALILNISEDHLDWHGsfEDYVaAKLKIFARQTEG--DVAVLNADDPRFA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 174 SKDIVNPVQYYGFDTakhapqlahyntegilcpkcEHILQYRLNTYanlgdficlncqfqrptldyqlteltaithqSSE 253
Cdd:TIGR01087 220 RLAQKSKAQVIWFSV--------------------EKDAERGLCIR-------------------------------DGG 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 407968025 254 FVIDGQNYKINVGGLYNIYNALAAVSVAEFFGVSPEKIKAGFNKSKAVFGRQETFK 309
Cdd:TIGR01087 249 LYLKPNDLEGSLLGLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYVG 304
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
50-306 |
2.81e-09 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 58.83 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 50 IVVITGTNGKTLTTALTVGILKEAFGDVLTnpsGANmitgITAAFLSAKKGKSGKHIAVLEIDEASLPKItNYLKPSLFV 129
Cdd:PRK14106 110 IVAITGTNGKTTTTTLLGEIFKNAGRKTLV---AGN----IGYPLIDAVEEYGEDDIIVAEVSSFQLETI-KEFKPKVGC 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 130 YTNIFRDQMDRYGEIyttyqmivDGARNApKATILANGDSPIFSSKDIVNPVqyygfdTAKHAPQLahyntegilcpKCE 209
Cdd:PRK14106 182 ILNITPDHLDRHKTM--------ENYIKA-KARIFENQRPSDYTVLNYDDPR------TRSLAKKA-----------KAR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 210 HILQYRLNTYANlGDFIclncqfqrptldyQLTELTAITHQSSEFVIDGQNYKINvgGLYNIYNALAAVSVAEFFGVSPE 289
Cdd:PRK14106 236 VIFFSRKSLLEE-GVFV-------------KNGKIVISLGGKEEEVIDIDEIFIP--GEHNLENALAATAAAYLLGISPD 299
|
250
....*....|....*..
gi 407968025 290 KIKAGFNKSKAVFGRQE 306
Cdd:PRK14106 300 VIANTLKTFKGVEHRIE 316
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
53-281 |
1.88e-08 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 54.23 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 53 ITGTNGKTLTTALTVGILKEAFGDVLT-----NPSGANMITGITAAFLSAKKGKSGKHIAVLEIDEASLPK--ITNYLKP 125
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLAGGVIGTigtyiGKSGNTTNNAIGLPLTLAEMVEAGAEYAVLEVSSHGLGEgrLSGLLKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 126 SLFVYTNIFRDQMDRYG---EIYTTYQMIVDGARNAPKATIlaNGDSPIFS-----SKDIVNPVQYYGFDTAKhapqlah 197
Cdd:pfam08245 81 DIAVFTNISPDHLDFHGtmeNYAKAKAELFEGLPEDGIAVI--NADDPYGAfliakLKKAGVRVITYGIEGEA------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 198 yntegilcpkcehilqyrlntyanlgdficlncqfqrptlDYQLTELTAiTHQSSEFVI---DGQNYKINVG--GLYNIY 272
Cdd:pfam08245 152 ----------------------------------------DLRAANIEL-SSDGTSFDLftvPGGELEIEIPllGRHNVY 190
|
....*....
gi 407968025 273 NALAAVSVA 281
Cdd:pfam08245 191 NALAAIAAA 199
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MurT_C |
pfam08353 |
MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from ... |
319-429 |
5.93e-44 |
|
MurT ligase C-terminal; This entry represents the C-terminal domain of MurT ligase from Gram-positive bacteria. MurT is part of the bi-enzymatic complex MurT-GatD involved in the amidation of the alpha-carboxyl group of the D-isoglutamate residue in Lipid II in the peptidoglycan layer to produce D-isoglutamine. This domain contains an aspartate at position 349, the third residue in the catalytic triad GatD-C94, GatD-H189, MurT-D349. This C-terminal domain is built around a central six-stranded, predominantly parallel beta-sheet that is sandwiched between four alpha-helices on one side and two alpha-helices on the other. The MurT-GatD heterodimer adopts a boomerang-shaped conformation, with GatD packing against the C-terminal domain of MurT.
Pssm-ID: 462442 Cd Length: 110 Bit Score: 149.56 E-value: 5.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 319 LIKNPVGASQALEMIQLADYPFSLSVLLNANYADGIDTSWIWDANFELITHMPITEINAGGVRHSEIARRLRVTGFDDTK 398
Cdd:pfam08353 1 LVKNPVGFNQVLNYIASDPGPKSLLLLLNDNYADGRDVSWIWDVDFEKLNDSNIKKIIVSGDRAYDMALRLKYAGVPEEK 80
|
90 100 110
....*....|....*....|....*....|.
gi 407968025 399 IKQAEKLEQITEAIeKQESKHAYILATYTAM 429
Cdd:pfam08353 81 IEIEEDLEEALDAI-KAPTENVYILPTYTAM 110
|
|
| MurC |
COG0773 |
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ... |
39-294 |
3.01e-15 |
|
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440536 [Multi-domain] Cd Length: 451 Bit Score: 77.41 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 39 DILDSLSKDYEIVVITGTNGKTLTTALTVGILKEAfgdvltnpsGAN---MITGITAAF-LSAKKGKSgkHIAVLEIDE- 113
Cdd:COG0773 95 EMLAELMRGKRSIAVAGTHGKTTTTSMLAHILEEA---------GLDptfLIGGILNNFgTNARLGDG--DYFVAEADEs 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 114 -ASLpkitNYLKPSLFVYTNIFRDQMDrygeIYTTYQMIVDG----ARNAPKA-TILANGDSPIfsSKDIV----NPVQY 183
Cdd:COG0773 164 dGSF----LHYSPDIAVVTNIEADHLD----IYGDLEAIKEAfhefARNVPFYgLLVLCADDPG--LRELLprcgRPVIT 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 184 YGFDtakhapqlahyntegilcpkcehilqyrlntyanlgdficlncqfqrPTLDYQLTELTAITHQSS-EFVIDGQNY- 261
Cdd:COG0773 234 YGFS-----------------------------------------------EDADYRAENIRIDGGGSTfDVLRRGEELg 266
|
250 260 270
....*....|....*....|....*....|....*
gi 407968025 262 --KINVGGLYNIYNALAAVSVAEFFGVSPEKIKAG 294
Cdd:COG0773 267 evELNLPGRHNVLNALAAIAVALELGVDPEAIAEA 301
|
|
| murD |
TIGR01087 |
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ... |
17-309 |
2.52e-14 |
|
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273436 [Multi-domain] Cd Length: 433 Bit Score: 74.68 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 17 LILKKLGRGSTYPGRLALAFDKDildslskDYEIVVITGTNGKTLTTALTVGILKEAFGDVltnPSGANmitgITAAFLS 96
Cdd:TIGR01087 78 LVQAAAKRGIPVVGDIELFLRLV-------PLPVVAITGTNGKTTTTSLLYHLLKAAGLKA---FLGGN----IGTPALE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 97 AKKGKsGKHIAVLEIDEASLpKITNYLKPSLFVYTNIFRDQMDRYG--EIYT-TYQMIVDGARNApkATILANGDSPIFS 173
Cdd:TIGR01087 144 VLDQE-GAELYVLELSSFQL-ETTESLRPEIALILNISEDHLDWHGsfEDYVaAKLKIFARQTEG--DVAVLNADDPRFA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 174 SKDIVNPVQYYGFDTakhapqlahyntegilcpkcEHILQYRLNTYanlgdficlncqfqrptldyqlteltaithqSSE 253
Cdd:TIGR01087 220 RLAQKSKAQVIWFSV--------------------EKDAERGLCIR-------------------------------DGG 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 407968025 254 FVIDGQNYKINVGGLYNIYNALAAVSVAEFFGVSPEKIKAGFNKSKAVFGRQETFK 309
Cdd:TIGR01087 249 LYLKPNDLEGSLLGLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYVG 304
|
|
| MurF |
COG0770 |
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
238-318 |
7.80e-11 |
|
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl pentapeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440533 [Multi-domain] Cd Length: 451 Bit Score: 63.58 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 238 DYQLTELTAiTHQSSEFVI----DGQNYKINVGGLYNIYNALAAVSVAEFFGVSPEKIKAGFNKSKAVFGRQETFKIGDk 313
Cdd:COG0770 245 DVRAEDIEL-DEDGTRFTLhtpgGELEVTLPLPGRHNVSNALAAAAVALALGLDLEEIAAGLAAFQPVKGRLEVIEGAG- 322
|
....*
gi 407968025 314 SCTLI 318
Cdd:COG0770 323 GVTLI 327
|
|
| murC |
TIGR01082 |
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial ... |
38-296 |
3.25e-10 |
|
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial peptidoglycan (murein) biosynthesis. In a few species (Mycobacterium leprae, the Chlamydia), the amino acid may be L-serine or glycine instead of L-alanine. A related protein, UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase (murein tripeptide ligase) is described by model TIGR01081. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273433 [Multi-domain] Cd Length: 448 Bit Score: 61.94 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 38 KDILDSLSKDYEIVVITGTNGKTLTTALTVGILKEAFGDvltnPSGAnmITGITAAF-LSAKKGKSGKHIAvlEIDE--A 114
Cdd:TIGR01082 89 AEMLAELMRFRHSIAVAGTHGKTTTTAMIAVILKEAGLD----PTVV--VGGLVKEAgTNARLGSGEYLVA--EADEsdA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 115 SLPKITnylkPSLFVYTNIFRDQMDRYGEIYTTY-QMIVDGARNAPKATIL-ANGDSPIFS--SKDIVNPVQYYGFDTAK 190
Cdd:TIGR01082 161 SFLHLQ----PNVAIVTNIEPDHLDTYGSSFERLkAAFEKFIHNLPFYGLAvICADDPVLRelVPKATEQVITYGGSGED 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 191 HAPQLAHYNTEGilcpkcehilqyrlntyaNLGDFiclncqfqrpTLDYQLTELTAIThqssefvidgqnykINVGGLYN 270
Cdd:TIGR01082 237 ADYRAENIQQSG------------------AEGKF----------SVRGKGKLYLEFT--------------LNLPGRHN 274
|
250 260
....*....|....*....|....*.
gi 407968025 271 IYNALAAVSVAEFFGVSPEKIKAGFN 296
Cdd:TIGR01082 275 VLNALAAIAVALELGIDFEAILRALA 300
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
50-294 |
6.43e-10 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 60.86 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 50 IVVITGTNGKTLTTALTVGILKEAFGDVltnPSGANmitgITAAFLSAKKGKSGKHIAVLE-----IDEaslpkiTNYLK 124
Cdd:COG0771 107 IIAITGTNGKTTTTTLIGHILKAAGLRV---AVGGN----IGTPLLDLLLEPEPPDVYVLElssfqLET------TPSLR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 125 PSLFVYTNIFRDQMDRYGEI--YttyqmivdgaRNApKATILANGDSPIFSskdIVN-------------PVQYYGFDTA 189
Cdd:COG0771 174 PDVAVILNITPDHLDRHGSMeaY----------AAA-KARIFANQTPDDYA---VLNaddpltralaeeaKARVVPFSLK 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 190 KHAPQLAHYNtEGILCpkcehilqyrlntYANLGDFIClncqfqrpTLDyqlteltaithqssefvidgqnyKINVGGLY 269
Cdd:COG0771 240 EPLEGGAGLE-DGKLV-------------DRASGEELL--------PVD-----------------------DLRLPGRH 274
|
250 260
....*....|....*....|....*
gi 407968025 270 NIYNALAAVSVAEFFGVSPEKIKAG 294
Cdd:COG0771 275 NLENALAALAAARALGVPPEAIREA 299
|
|
| murF |
TIGR01143 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the ... |
49-318 |
1.40e-09 |
|
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the strictly bacterial MurF gene of peptidoglycan biosynthesis. This enzyme is almost always UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanyl ligase, but in a few species, MurE adds lysine rather than diaminopimelate. This enzyme acts on the product from MurE activity, and so is also subfamily rather than equivalog. Staphylococcus aureus is an example of species in this MurF protein would differ. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273468 [Multi-domain] Cd Length: 417 Bit Score: 59.59 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 49 EIVVITGTNGKTLTTALTVGILKEAFGDVLTNPSGANMItGITAAFLSAkkgkSGKH-IAVLEI------DEASLPKItn 121
Cdd:TIGR01143 75 KVIGITGSSGKTTTKEMLAAILSHKYKVFATPGNFNNEI-GLPLTLLRA----PGDHdYAVLEMgashpgEIAYLAEI-- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 122 yLKPSLFVYTNIFRDQMDRYG----------EIYttyqmivdgARNAPKATILANGDSPIFS--SKDIVN-PVQYYGFDT 188
Cdd:TIGR01143 148 -AKPDIAVITNIGPAHLEGFGslegiaeakgEIL---------QGLKENGIAVINADDPAFAdlAKRLPNrNILSFGFEG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 189 AKHAPQLAHYNTEGilcpkCEHIlqyrlntyanlgDFICLNCQFqrptldyqlteltaithqssefvidgqNYKINVGGL 268
Cdd:TIGR01143 218 GDFVAKDISYSALG-----STSF------------TLVAPGGEF---------------------------EVSLPLLGR 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 407968025 269 YNIYNALAAVSVAEFFGVSPEKIKAGFNKSKAVFGRQETfkIGDKSCTLI 318
Cdd:TIGR01143 254 HNVMNALAAAALALELGIPLEEIAEGLAELKLVKGRFEV--QTKNGLTLI 301
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
50-306 |
2.81e-09 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 58.83 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 50 IVVITGTNGKTLTTALTVGILKEAFGDVLTnpsGANmitgITAAFLSAKKGKSGKHIAVLEIDEASLPKItNYLKPSLFV 129
Cdd:PRK14106 110 IVAITGTNGKTTTTTLLGEIFKNAGRKTLV---AGN----IGYPLIDAVEEYGEDDIIVAEVSSFQLETI-KEFKPKVGC 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 130 YTNIFRDQMDRYGEIyttyqmivDGARNApKATILANGDSPIFSSKDIVNPVqyygfdTAKHAPQLahyntegilcpKCE 209
Cdd:PRK14106 182 ILNITPDHLDRHKTM--------ENYIKA-KARIFENQRPSDYTVLNYDDPR------TRSLAKKA-----------KAR 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 210 HILQYRLNTYANlGDFIclncqfqrptldyQLTELTAITHQSSEFVIDGQNYKINvgGLYNIYNALAAVSVAEFFGVSPE 289
Cdd:PRK14106 236 VIFFSRKSLLEE-GVFV-------------KNGKIVISLGGKEEEVIDIDEIFIP--GEHNLENALAATAAAYLLGISPD 299
|
250
....*....|....*..
gi 407968025 290 KIKAGFNKSKAVFGRQE 306
Cdd:PRK14106 300 VIANTLKTFKGVEHRIE 316
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
53-281 |
1.88e-08 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 54.23 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 53 ITGTNGKTLTTALTVGILKEAFGDVLT-----NPSGANMITGITAAFLSAKKGKSGKHIAVLEIDEASLPK--ITNYLKP 125
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLAGGVIGTigtyiGKSGNTTNNAIGLPLTLAEMVEAGAEYAVLEVSSHGLGEgrLSGLLKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 126 SLFVYTNIFRDQMDRYG---EIYTTYQMIVDGARNAPKATIlaNGDSPIFS-----SKDIVNPVQYYGFDTAKhapqlah 197
Cdd:pfam08245 81 DIAVFTNISPDHLDFHGtmeNYAKAKAELFEGLPEDGIAVI--NADDPYGAfliakLKKAGVRVITYGIEGEA------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 198 yntegilcpkcehilqyrlntyanlgdficlncqfqrptlDYQLTELTAiTHQSSEFVI---DGQNYKINVG--GLYNIY 272
Cdd:pfam08245 152 ----------------------------------------DLRAANIEL-SSDGTSFDLftvPGGELEIEIPllGRHNVY 190
|
....*....
gi 407968025 273 NALAAVSVA 281
Cdd:pfam08245 191 NALAAIAAA 199
|
|
| MurE |
COG0769 |
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
238-313 |
2.63e-08 |
|
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl tripeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440532 [Multi-domain] Cd Length: 459 Bit Score: 55.86 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 238 DYQLTELTaITHQSSEFVID--GQNYKINVG--GLYNIYNALAAVSVAEFFGVSPEKIKAGFNKSKAVFGRQETFKIGDK 313
Cdd:COG0769 239 DLRATDIE-LSADGTRFTLVtpGGEVEVRLPliGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPGRMERVDGGQG 317
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
50-346 |
5.89e-08 |
|
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;
Pssm-ID: 237025 [Multi-domain] Cd Length: 958 Bit Score: 55.10 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 50 IVVITGTNGKTLTTALTVGILKEAFGD--VLTNPSGANMITGITAAFLSAKKGKsgkHIAVLEIDEASLPKITnYL---- 123
Cdd:PRK11929 605 VVAITGSNGKTTTKEMIAAILAAWQGEdrVLATEGNFNNEIGVPLTLLRLRAQH---RAAVFELGMNHPGEIA-YLaaia 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 124 KPSLFVYTNIFRDQMDRYGEIyttyqmivDGarnapkatiLANGDSPIFSSKdIVNPVQYYGFD---TAKHAPQLAHYNT 200
Cdd:PRK11929 681 APTVALVTNAQREHQEFMHSV--------EA---------VARAKGEIIAAL-PEDGVAVVNGDdpyTAIWAKLAGARRV 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407968025 201 egilcpkCEHILQYRLNTYANlgDFICLNCQFQRPTLDYQLTeltaITHQSSEFVIdgqnykiNVGGLYNIYNALAAVSV 280
Cdd:PRK11929 743 -------LRFGLQPGADVYAE--KIAKDISVGEAGGTRCQVV----TPAGSAEVYL-------PLIGEHNLRNALAAIAC 802
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407968025 281 AEFFGVSPEKIKAGFNKSKAVFGRQETFKIgdkSCTLILI-----KNPVGASQALEMiqLADYPFSLSVLL 346
Cdd:PRK11929 803 ALAAGASLKQIRAGLERFQPVAGRMQRRRL---SCGTRIIddtynANPDSMRAAIDV--LAELPNGPRALV 868
|
|
| murE |
PRK00139 |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional |
238-313 |
4.00e-06 |
|
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
Pssm-ID: 234660 [Multi-domain] Cd Length: 460 Bit Score: 48.97 E-value: 4.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407968025 238 DYQLTELTaITHQSSEFVIDGQnYKINVGGLYNIYNALAAVSVAEFFGVSPEKIKAGFNKSKAVFGRQETFKIGDK 313
Cdd:PRK00139 249 DLRATDVE-YTDSGQTFTLVTE-VESPLIGRFNVSNLLAALAALLALGVPLEDALAALAKLQGVPGRMERVDAGQG 322
|
|
|