NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|504872889|ref|WP_015059991|]
View 

MULTISPECIES: OXA-48 family carbapenem-hydrolyzing class D beta-lactamase OXA-48 [Gammaproteobacteria]

Protein Classification

class D beta-lactamase( domain architecture ID 10006473)

class D beta-lactamase hydrolyzes the amide bond of the beta-lactam ring via the formation of an acyl-enzyme covalent complex

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
YbxI COG2602
Beta-lactamase class D [Defense mechanisms];
1-265 1.36e-142

Beta-lactamase class D [Defense mechanisms];


:

Pssm-ID: 442014 [Multi-domain]  Cd Length: 267  Bit Score: 400.80  E-value: 1.36e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889   1 MR--VLALSAVFLVASIIGMPAVAKEWQENKSWNAHFTEHKSQGVVVLWNENKQQGFTNNLKRANQAFLPASTFKIPNSL 78
Cdd:COG2602    1 MKklLLLLALLLLLACPANAAAAAANVIERPDLAKLFDEAGVEGTFVLYDLKTGKYIVYNKERAETRFSPASTFKIPNSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889  79 IALDLGVVKDEHQVFKWDGQTRDIATWNRDHNLITAMKYSVVPVYQEFARQIGEARMSKMLHAFDYGNEDISGNVDSFWL 158
Cdd:COG2602   81 IALETGVIKDENEVFKWDGVKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKYLDKLNYGNADISGGIDTFWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889 159 DGGIRISATEQISFLRKLYHNKLHVSERSQRIVKQAMLTEANGDYIIRAKTGYSTRIEPKIGWWVGWVELDDNVWFFAMN 238
Cdd:COG2602  161 DGSLKISALEQIDFLKRLYRNKLPFSKRTQDIVKDIMIVEKTPNYTLYGKTGWGFRDDPDIGWFVGWVEKNDNVYFFATN 240
                        250       260
                 ....*....|....*....|....*..
gi 504872889 239 MDMPTSDGLGLRQAITKEVLKQEKIIP 265
Cdd:COG2602  241 IDIPDEADLPKRKEITRKILKQLGLLP 267
 
Name Accession Description Interval E-value
YbxI COG2602
Beta-lactamase class D [Defense mechanisms];
1-265 1.36e-142

Beta-lactamase class D [Defense mechanisms];


Pssm-ID: 442014 [Multi-domain]  Cd Length: 267  Bit Score: 400.80  E-value: 1.36e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889   1 MR--VLALSAVFLVASIIGMPAVAKEWQENKSWNAHFTEHKSQGVVVLWNENKQQGFTNNLKRANQAFLPASTFKIPNSL 78
Cdd:COG2602    1 MKklLLLLALLLLLACPANAAAAAANVIERPDLAKLFDEAGVEGTFVLYDLKTGKYIVYNKERAETRFSPASTFKIPNSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889  79 IALDLGVVKDEHQVFKWDGQTRDIATWNRDHNLITAMKYSVVPVYQEFARQIGEARMSKMLHAFDYGNEDISGNVDSFWL 158
Cdd:COG2602   81 IALETGVIKDENEVFKWDGVKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKYLDKLNYGNADISGGIDTFWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889 159 DGGIRISATEQISFLRKLYHNKLHVSERSQRIVKQAMLTEANGDYIIRAKTGYSTRIEPKIGWWVGWVELDDNVWFFAMN 238
Cdd:COG2602  161 DGSLKISALEQIDFLKRLYRNKLPFSKRTQDIVKDIMIVEKTPNYTLYGKTGWGFRDDPDIGWFVGWVEKNDNVYFFATN 240
                        250       260
                 ....*....|....*....|....*..
gi 504872889 239 MDMPTSDGLGLRQAITKEVLKQEKIIP 265
Cdd:COG2602  241 IDIPDEADLPKRKEITRKILKQLGLLP 267
Transpeptidase pfam00905
Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss: ...
48-259 5.41e-42

Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss:P14677) is conserved in all members of this family.


Pssm-ID: 425939 [Multi-domain]  Cd Length: 296  Bit Score: 145.25  E-value: 5.41e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889   48 NENKQQGFTNNlKRANQAFLPASTFKIPNSLIALDLGVVKDEHQVFKWDG---QTRDIATWNRDH----NLITAMKYSVV 120
Cdd:pfam00905  23 DPNGFIGPLRN-RAVTSRYEPGSTFKPFTALAALDNGVLKPDETIFDWPGkqqGGKSIGDWNQDQvgigTLRQALEYSSN 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889  121 PVYQEFARQIGEARMSKMLHAFDYGNED-------ISGNVDSFWLDG-------GIRISATEQISFLRKLYH-------- 178
Cdd:pfam00905 102 WYMQKLAQKLGADKLRSYLKKFGYGNKTgiglpgeNAGYLTPYWLEGatasfgiGLTITPLQQAQAYAAIANggklvpph 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889  179 --------------NKLHVSERSQRIVKQAMLTEANGD----------YIIRAKTG---------YSTRIEPKIGWWVGW 225
Cdd:pfam00905 182 lvksiedkvdpkvlNKLPISKSTAEKVKDMLRLVVNDGtgtgtaavpgYKVAGKTGtaqvagpkgGGYYDGAQIGWFVGY 261
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 504872889  226 VELDDNVWFFAMNMDMPT-SDGLGLRQAITKEVLK 259
Cdd:pfam00905 262 APADNPKYAFAVLIDDPKrYYGGKVAAPIFKDILE 296
pbp2_mrdA TIGR03423
penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 ...
35-151 9.46e-06

penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 (PBP-2), a protein whose gene (designated pbpA or mrdA) generally is found next to the gene for RodA, a protein required for rod (bacillus) shape in many bacteria. PBP-2 acts as a transpeptidase for cell elongation (hence, rod-shape). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 274573 [Multi-domain]  Cd Length: 592  Bit Score: 46.36  E-value: 9.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889   35 FTEHKSQGVVVLWNENKQQGFTNnlkRANQA-FLPASTFKIPNSLIALDLGVVKDEHQV-----FKWDGQT-RDiatWNR 107
Cdd:TIGR03423 275 FVDGISSKDYKALLNDPDRPLLN---RAIQGvYPPGSTFKPVVALAALEEGVITPETRIycpgyFQLGGRRfRC---WKR 348
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 504872889  108 -DH---NLITAMKYSVVPVYQEFARQIGEARMSKMLHAFDYGNE---DISG 151
Cdd:TIGR03423 349 gGHgrvDLRKAIEESCDVYFYQLALRLGIDKIAEYAKRFGFGQKtgiDLPG 399
 
Name Accession Description Interval E-value
YbxI COG2602
Beta-lactamase class D [Defense mechanisms];
1-265 1.36e-142

Beta-lactamase class D [Defense mechanisms];


Pssm-ID: 442014 [Multi-domain]  Cd Length: 267  Bit Score: 400.80  E-value: 1.36e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889   1 MR--VLALSAVFLVASIIGMPAVAKEWQENKSWNAHFTEHKSQGVVVLWNENKQQGFTNNLKRANQAFLPASTFKIPNSL 78
Cdd:COG2602    1 MKklLLLLALLLLLACPANAAAAAANVIERPDLAKLFDEAGVEGTFVLYDLKTGKYIVYNKERAETRFSPASTFKIPNSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889  79 IALDLGVVKDEHQVFKWDGQTRDIATWNRDHNLITAMKYSVVPVYQEFARQIGEARMSKMLHAFDYGNEDISGNVDSFWL 158
Cdd:COG2602   81 IALETGVIKDENEVFKWDGVKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKYLDKLNYGNADISGGIDTFWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889 159 DGGIRISATEQISFLRKLYHNKLHVSERSQRIVKQAMLTEANGDYIIRAKTGYSTRIEPKIGWWVGWVELDDNVWFFAMN 238
Cdd:COG2602  161 DGSLKISALEQIDFLKRLYRNKLPFSKRTQDIVKDIMIVEKTPNYTLYGKTGWGFRDDPDIGWFVGWVEKNDNVYFFATN 240
                        250       260
                 ....*....|....*....|....*..
gi 504872889 239 MDMPTSDGLGLRQAITKEVLKQEKIIP 265
Cdd:COG2602  241 IDIPDEADLPKRKEITRKILKQLGLLP 267
Transpeptidase pfam00905
Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss: ...
48-259 5.41e-42

Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss:P14677) is conserved in all members of this family.


Pssm-ID: 425939 [Multi-domain]  Cd Length: 296  Bit Score: 145.25  E-value: 5.41e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889   48 NENKQQGFTNNlKRANQAFLPASTFKIPNSLIALDLGVVKDEHQVFKWDG---QTRDIATWNRDH----NLITAMKYSVV 120
Cdd:pfam00905  23 DPNGFIGPLRN-RAVTSRYEPGSTFKPFTALAALDNGVLKPDETIFDWPGkqqGGKSIGDWNQDQvgigTLRQALEYSSN 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889  121 PVYQEFARQIGEARMSKMLHAFDYGNED-------ISGNVDSFWLDG-------GIRISATEQISFLRKLYH-------- 178
Cdd:pfam00905 102 WYMQKLAQKLGADKLRSYLKKFGYGNKTgiglpgeNAGYLTPYWLEGatasfgiGLTITPLQQAQAYAAIANggklvpph 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889  179 --------------NKLHVSERSQRIVKQAMLTEANGD----------YIIRAKTG---------YSTRIEPKIGWWVGW 225
Cdd:pfam00905 182 lvksiedkvdpkvlNKLPISKSTAEKVKDMLRLVVNDGtgtgtaavpgYKVAGKTGtaqvagpkgGGYYDGAQIGWFVGY 261
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 504872889  226 VELDDNVWFFAMNMDMPT-SDGLGLRQAITKEVLK 259
Cdd:pfam00905 262 APADNPKYAFAVLIDDPKrYYGGKVAAPIFKDILE 296
pbp2_mrdA TIGR03423
penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 ...
35-151 9.46e-06

penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 (PBP-2), a protein whose gene (designated pbpA or mrdA) generally is found next to the gene for RodA, a protein required for rod (bacillus) shape in many bacteria. PBP-2 acts as a transpeptidase for cell elongation (hence, rod-shape). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 274573 [Multi-domain]  Cd Length: 592  Bit Score: 46.36  E-value: 9.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889   35 FTEHKSQGVVVLWNENKQQGFTNnlkRANQA-FLPASTFKIPNSLIALDLGVVKDEHQV-----FKWDGQT-RDiatWNR 107
Cdd:TIGR03423 275 FVDGISSKDYKALLNDPDRPLLN---RAIQGvYPPGSTFKPVVALAALEEGVITPETRIycpgyFQLGGRRfRC---WKR 348
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 504872889  108 -DH---NLITAMKYSVVPVYQEFARQIGEARMSKMLHAFDYGNE---DISG 151
Cdd:TIGR03423 349 gGHgrvDLRKAIEESCDVYFYQLALRLGIDKIAEYAKRFGFGQKtgiDLPG 399
FtsI COG0768
Cell division protein FtsI, peptidoglycan transpeptidase (Penicillin-binding protein 2) [Cell ...
68-145 3.56e-05

Cell division protein FtsI, peptidoglycan transpeptidase (Penicillin-binding protein 2) [Cell cycle control, cell division, chromosome partitioning, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440531 [Multi-domain]  Cd Length: 568  Bit Score: 44.82  E-value: 3.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504872889  68 PASTFKIPNSLIALDLGVVkDEHQVFKWDGQ----TRDIATWNRDH----NLITAMKYSVVPVYQEFARQIGEARMSKML 139
Cdd:COG0768  294 PGSTFKPFTAAAALEEGVI-TPDTTFDCPGYyrvgGRTIRDWDRGGhgtlTLTEALAKSSNVGFYKLALRLGIDKLYDYL 372

                 ....*.
gi 504872889 140 HAFDYG 145
Cdd:COG0768  373 KKFGLG 378
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH