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Conserved domains on  [gi|1628767365|gb|QCH41476|]
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carbapenem-hydrolyzing class D beta-lactamase OXA-51 [Cloning vector pET28A-blaOXA-51]

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

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List of domain hits

Name Accession Description Interval E-value
YbxI COG2602
Beta-lactamase class D [Defense mechanisms];
4-274 2.87e-111

Beta-lactamase class D [Defense mechanisms];


:

Pssm-ID: 442014 [Multi-domain]  Cd Length: 267  Bit Score: 321.83  E-value: 2.87e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365   4 KTLLLITSAIFISACSPYIvtanpnHSASKSDEKAEKIKNLFNEVHTTGVLVIQQGQTQQSYGNDLARASTEYVPASTFK 83
Cdd:COG2602     2 KKLLLLLALLLLLACPANA------AAAAANVIERPDLAKLFDEAGVEGTFVLYDLKTGKYIVYNKERAETRFSPASTFK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365  84 MLNALIGLEHHKATTT-EVFKWDGQKRLFPEWEKDMTLGDAMKASAIPVYQDLARRIGLELMSKEVKRVGYGNADIGTQV 162
Cdd:COG2602    76 IPNSLIALETGVIKDEnEVFKWDGVKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKYLDKLNYGNADISGGI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365 163 DNFWLVGPLKITPQQEAQFAYKLANKTLPFSPKVQDEVQSMLFIEEKNGNKIYAKSGWGWDVDPQVGWLTGWVVQPqGNI 242
Cdd:COG2602   156 DTFWLDGSLKISALEQIDFLKRLYRNKLPFSKRTQDIVKDIMIVEKTPNYTLYGKTGWGFRDDPDIGWFVGWVEKN-DNV 234
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1628767365 243 VAFSLNLEMKKGIPSSVRKEITYKSLEQLGIL 274
Cdd:COG2602   235 YFFATNIDIPDEADLPKRKEITRKILKQLGLL 266
 
Name Accession Description Interval E-value
YbxI COG2602
Beta-lactamase class D [Defense mechanisms];
4-274 2.87e-111

Beta-lactamase class D [Defense mechanisms];


Pssm-ID: 442014 [Multi-domain]  Cd Length: 267  Bit Score: 321.83  E-value: 2.87e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365   4 KTLLLITSAIFISACSPYIvtanpnHSASKSDEKAEKIKNLFNEVHTTGVLVIQQGQTQQSYGNDLARASTEYVPASTFK 83
Cdd:COG2602     2 KKLLLLLALLLLLACPANA------AAAAANVIERPDLAKLFDEAGVEGTFVLYDLKTGKYIVYNKERAETRFSPASTFK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365  84 MLNALIGLEHHKATTT-EVFKWDGQKRLFPEWEKDMTLGDAMKASAIPVYQDLARRIGLELMSKEVKRVGYGNADIGTQV 162
Cdd:COG2602    76 IPNSLIALETGVIKDEnEVFKWDGVKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKYLDKLNYGNADISGGI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365 163 DNFWLVGPLKITPQQEAQFAYKLANKTLPFSPKVQDEVQSMLFIEEKNGNKIYAKSGWGWDVDPQVGWLTGWVVQPqGNI 242
Cdd:COG2602   156 DTFWLDGSLKISALEQIDFLKRLYRNKLPFSKRTQDIVKDIMIVEKTPNYTLYGKTGWGFRDDPDIGWFVGWVEKN-DNV 234
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1628767365 243 VAFSLNLEMKKGIPSSVRKEITYKSLEQLGIL 274
Cdd:COG2602   235 YFFATNIDIPDEADLPKRKEITRKILKQLGLL 266
Transpeptidase pfam00905
Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss: ...
50-269 1.78e-29

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: 112.89  E-value: 1.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365  50 TTGVLVIQQGQTQ---QSYGNDLARASTE-YVPASTFKMLNALIGLEHHKATTTEVFK-WDGQKR---LFPEWEKDM--- 118
Cdd:pfam00905  10 TGEVLAMVGKPSYdpnGFIGPLRNRAVTSrYEPGSTFKPFTALAALDNGVLKPDETIFdWPGKQQggkSIGDWNQDQvgi 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365 119 -TLGDAMKASAIPVYQDLARRIGLELMSKEVKRVGYGNAD-------IGTQVDNFWLVGP-------LKITPQQEAQFAY 183
Cdd:pfam00905  90 gTLRQALEYSSNWYMQKLAQKLGADKLRSYLKKFGYGNKTgiglpgeNAGYLTPYWLEGAtasfgigLTITPLQQAQAYA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365 184 KLAN----------------------KTLPFSPKVQDEVQSMLFIEEKNGN----------KIYAKSGW---------GW 222
Cdd:pfam00905 170 AIANggklvpphlvksiedkvdpkvlNKLPISKSTAEKVKDMLRLVVNDGTgtgtaavpgyKVAGKTGTaqvagpkggGY 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1628767365 223 DVDPQVGWLTGWVVQpQGNIVAFSLNLEMKKGI-PSSVRKEITYKSLE 269
Cdd:pfam00905 250 YDGAQIGWFVGYAPA-DNPKYAFAVLIDDPKRYyGGKVAAPIFKDILE 296
pbp2_mrdA TIGR03423
penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 ...
76-154 8.97e-07

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: 49.83  E-value: 8.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365  76 YVPASTFKMLNALIGLEHHKATTTEVF----KWDGQKRLFPEWEK----DMTLGDAMKASAIPVYQDLARRIGLELMSKE 147
Cdd:TIGR03423 304 YPPGSTFKPVVALAALEEGVITPETRIycpgYFQLGGRRFRCWKRgghgRVDLRKAIEESCDVYFYQLALRLGIDKIAEY 383

                  ....*..
gi 1628767365 148 VKRVGYG 154
Cdd:TIGR03423 384 AKRFGFG 390
 
Name Accession Description Interval E-value
YbxI COG2602
Beta-lactamase class D [Defense mechanisms];
4-274 2.87e-111

Beta-lactamase class D [Defense mechanisms];


Pssm-ID: 442014 [Multi-domain]  Cd Length: 267  Bit Score: 321.83  E-value: 2.87e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365   4 KTLLLITSAIFISACSPYIvtanpnHSASKSDEKAEKIKNLFNEVHTTGVLVIQQGQTQQSYGNDLARASTEYVPASTFK 83
Cdd:COG2602     2 KKLLLLLALLLLLACPANA------AAAAANVIERPDLAKLFDEAGVEGTFVLYDLKTGKYIVYNKERAETRFSPASTFK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365  84 MLNALIGLEHHKATTT-EVFKWDGQKRLFPEWEKDMTLGDAMKASAIPVYQDLARRIGLELMSKEVKRVGYGNADIGTQV 162
Cdd:COG2602    76 IPNSLIALETGVIKDEnEVFKWDGVKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKYLDKLNYGNADISGGI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365 163 DNFWLVGPLKITPQQEAQFAYKLANKTLPFSPKVQDEVQSMLFIEEKNGNKIYAKSGWGWDVDPQVGWLTGWVVQPqGNI 242
Cdd:COG2602   156 DTFWLDGSLKISALEQIDFLKRLYRNKLPFSKRTQDIVKDIMIVEKTPNYTLYGKTGWGFRDDPDIGWFVGWVEKN-DNV 234
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1628767365 243 VAFSLNLEMKKGIPSSVRKEITYKSLEQLGIL 274
Cdd:COG2602   235 YFFATNIDIPDEADLPKRKEITRKILKQLGLL 266
Transpeptidase pfam00905
Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss: ...
50-269 1.78e-29

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: 112.89  E-value: 1.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365  50 TTGVLVIQQGQTQ---QSYGNDLARASTE-YVPASTFKMLNALIGLEHHKATTTEVFK-WDGQKR---LFPEWEKDM--- 118
Cdd:pfam00905  10 TGEVLAMVGKPSYdpnGFIGPLRNRAVTSrYEPGSTFKPFTALAALDNGVLKPDETIFdWPGKQQggkSIGDWNQDQvgi 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365 119 -TLGDAMKASAIPVYQDLARRIGLELMSKEVKRVGYGNAD-------IGTQVDNFWLVGP-------LKITPQQEAQFAY 183
Cdd:pfam00905  90 gTLRQALEYSSNWYMQKLAQKLGADKLRSYLKKFGYGNKTgiglpgeNAGYLTPYWLEGAtasfgigLTITPLQQAQAYA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365 184 KLAN----------------------KTLPFSPKVQDEVQSMLFIEEKNGN----------KIYAKSGW---------GW 222
Cdd:pfam00905 170 AIANggklvpphlvksiedkvdpkvlNKLPISKSTAEKVKDMLRLVVNDGTgtgtaavpgyKVAGKTGTaqvagpkggGY 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1628767365 223 DVDPQVGWLTGWVVQpQGNIVAFSLNLEMKKGI-PSSVRKEITYKSLE 269
Cdd:pfam00905 250 YDGAQIGWFVGYAPA-DNPKYAFAVLIDDPKRYyGGKVAAPIFKDILE 296
FtsI COG0768
Cell division protein FtsI, peptidoglycan transpeptidase (Penicillin-binding protein 2) [Cell ...
71-154 3.84e-08

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: 53.67  E-value: 3.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365  71 RA-STEYVPASTFKMLNALIGLEHHKATTTEVFKWDGQ----KRLFPEWEK----DMTLGDAMKASA-IPVYQdLARRIG 140
Cdd:COG0768   286 RAvQGTYEPGSTFKPFTAAAALEEGVITPDTTFDCPGYyrvgGRTIRDWDRgghgTLTLTEALAKSSnVGFYK-LALRLG 364
                          90
                  ....*....|....
gi 1628767365 141 LELMSKEVKRVGYG 154
Cdd:COG0768   365 IDKLYDYLKKFGLG 378
pbp2_mrdA TIGR03423
penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 ...
76-154 8.97e-07

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: 49.83  E-value: 8.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1628767365  76 YVPASTFKMLNALIGLEHHKATTTEVF----KWDGQKRLFPEWEK----DMTLGDAMKASAIPVYQDLARRIGLELMSKE 147
Cdd:TIGR03423 304 YPPGSTFKPVVALAALEEGVITPETRIycpgYFQLGGRRFRCWKRgghgRVDLRKAIEESCDVYFYQLALRLGIDKIAEY 383

                  ....*..
gi 1628767365 148 VKRVGYG 154
Cdd:TIGR03423 384 AKRFGFG 390
 
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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