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Conserved domains on  [gi|60391844|sp|P0A1V9|]
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RecName: Full=Beta-lactamase OXA-2; AltName: Full=Penicillinase; Flags: Precursor

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];
3-264 3.21e-128

Beta-lactamase class D [Defense mechanisms];


:

Pssm-ID: 442014 [Multi-domain]  Cd Length: 267  Bit Score: 364.59  E-value: 3.21e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844   3 IRIFAILFSIFSLATFAHAQEGTL-ERSDWRKFFSEFQAKGTIVVADERqaDRAMLVFDPVRSKKRYSPASTFKIPHTLF 81
Cdd:COG2602   4 LLLLLALLLLLACPANAAAAAANViERPDLAKLFDEAGVEGTFVLYDLK--TGKYIVYNKERAETRFSPASTFKIPNSLI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844  82 ALDAGAVRDEFQIFRWDGVNRGFAGHNQDQDLRSAMRNSTVWVYELFAKEIGDDKARRYLKKIDYGNADPSTSNGDYWIE 161
Cdd:COG2602  82 ALETGVIKDENEVFKWDGVKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKYLDKLNYGNADISGGIDTFWLD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844 162 GSLAISAQEQIAFLRKLYRNELPFRVEHQRLVKDLMIVEAGRNWILRAKTGW----EGRMGWWVGWVEWPTGSVFFALNI 237
Cdd:COG2602 162 GSLKISALEQIDFLKRLYRNKLPFSKRTQDIVKDIMIVEKTPNYTLYGKTGWgfrdDPDIGWFVGWVEKNDNVYFFATNI 241
                       250       260
                ....*....|....*....|....*..
gi 60391844 238 DTPNRmDDLFKREAIVRAILRSIEALP 264
Cdd:COG2602 242 DIPDE-ADLPKRKEITRKILKQLGLLP 267
 
Name Accession Description Interval E-value
YbxI COG2602
Beta-lactamase class D [Defense mechanisms];
3-264 3.21e-128

Beta-lactamase class D [Defense mechanisms];


Pssm-ID: 442014 [Multi-domain]  Cd Length: 267  Bit Score: 364.59  E-value: 3.21e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844   3 IRIFAILFSIFSLATFAHAQEGTL-ERSDWRKFFSEFQAKGTIVVADERqaDRAMLVFDPVRSKKRYSPASTFKIPHTLF 81
Cdd:COG2602   4 LLLLLALLLLLACPANAAAAAANViERPDLAKLFDEAGVEGTFVLYDLK--TGKYIVYNKERAETRFSPASTFKIPNSLI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844  82 ALDAGAVRDEFQIFRWDGVNRGFAGHNQDQDLRSAMRNSTVWVYELFAKEIGDDKARRYLKKIDYGNADPSTSNGDYWIE 161
Cdd:COG2602  82 ALETGVIKDENEVFKWDGVKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKYLDKLNYGNADISGGIDTFWLD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844 162 GSLAISAQEQIAFLRKLYRNELPFRVEHQRLVKDLMIVEAGRNWILRAKTGW----EGRMGWWVGWVEWPTGSVFFALNI 237
Cdd:COG2602 162 GSLKISALEQIDFLKRLYRNKLPFSKRTQDIVKDIMIVEKTPNYTLYGKTGWgfrdDPDIGWFVGWVEKNDNVYFFATNI 241
                       250       260
                ....*....|....*....|....*..
gi 60391844 238 DTPNRmDDLFKREAIVRAILRSIEALP 264
Cdd:COG2602 242 DIPDE-ADLPKRKEITRKILKQLGLLP 267
Transpeptidase pfam00905
Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss: ...
42-257 1.26e-51

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: 170.67  E-value: 1.26e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844    42 GTIVVADERQADRAMLVFDPVR-------------SKKRYSPASTFKIPHTLFALDAGAVRDEFQIFRWDGVNRG---FA 105
Cdd:pfam00905   1 GSAVVLDPKTGEVLAMVGKPSYdpngfigplrnraVTSRYEPGSTFKPFTALAALDNGVLKPDETIFDWPGKQQGgksIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844   106 GHNQDQ----DLRSAMRNSTVWVYELFAKEIGDDKARRYLKKIDYGNAD----PSTSNG---DYWIEGS-------LAIS 167
Cdd:pfam00905  81 DWNQDQvgigTLRQALEYSSNWYMQKLAQKLGADKLRSYLKKFGYGNKTgiglPGENAGyltPYWLEGAtasfgigLTIT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844   168 AQEQIAFLRKLYR----------------------NELPFRVEHQRLVKDLMIVEAGRN----------WILRAKTGWEG 215
Cdd:pfam00905 161 PLQQAQAYAAIANggklvpphlvksiedkvdpkvlNKLPISKSTAEKVKDMLRLVVNDGtgtgtaavpgYKVAGKTGTAQ 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 60391844   216 RMG-------------WWVGWVEWPTGSVFFALNIDTPNRMDDLFKREAIVRAIL 257
Cdd:pfam00905 241 VAGpkgggyydgaqigWFVGYAPADNPKYAFAVLIDDPKRYYGGKVAAPIFKDIL 295
pbp2_mrdA TIGR03423
penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 ...
68-147 4.54e-05

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: 44.44  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844    68 YSPASTFKIPHTLFALDAGAVRDEFQIF---RWDGVNRGF-----AGHNqDQDLRSAMRNST-VWVYELfAKEIGDDKAR 138
Cdd:TIGR03423 304 YPPGSTFKPVVALAALEEGVITPETRIYcpgYFQLGGRRFrcwkrGGHG-RVDLRKAIEESCdVYFYQL-ALRLGIDKIA 381

                  ....*....
gi 60391844   139 RYLKKIDYG 147
Cdd:TIGR03423 382 EYAKRFGFG 390
 
Name Accession Description Interval E-value
YbxI COG2602
Beta-lactamase class D [Defense mechanisms];
3-264 3.21e-128

Beta-lactamase class D [Defense mechanisms];


Pssm-ID: 442014 [Multi-domain]  Cd Length: 267  Bit Score: 364.59  E-value: 3.21e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844   3 IRIFAILFSIFSLATFAHAQEGTL-ERSDWRKFFSEFQAKGTIVVADERqaDRAMLVFDPVRSKKRYSPASTFKIPHTLF 81
Cdd:COG2602   4 LLLLLALLLLLACPANAAAAAANViERPDLAKLFDEAGVEGTFVLYDLK--TGKYIVYNKERAETRFSPASTFKIPNSLI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844  82 ALDAGAVRDEFQIFRWDGVNRGFAGHNQDQDLRSAMRNSTVWVYELFAKEIGDDKARRYLKKIDYGNADPSTSNGDYWIE 161
Cdd:COG2602  82 ALETGVIKDENEVFKWDGVKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKYLDKLNYGNADISGGIDTFWLD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844 162 GSLAISAQEQIAFLRKLYRNELPFRVEHQRLVKDLMIVEAGRNWILRAKTGW----EGRMGWWVGWVEWPTGSVFFALNI 237
Cdd:COG2602 162 GSLKISALEQIDFLKRLYRNKLPFSKRTQDIVKDIMIVEKTPNYTLYGKTGWgfrdDPDIGWFVGWVEKNDNVYFFATNI 241
                       250       260
                ....*....|....*....|....*..
gi 60391844 238 DTPNRmDDLFKREAIVRAILRSIEALP 264
Cdd:COG2602 242 DIPDE-ADLPKRKEITRKILKQLGLLP 267
Transpeptidase pfam00905
Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss: ...
42-257 1.26e-51

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: 170.67  E-value: 1.26e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844    42 GTIVVADERQADRAMLVFDPVR-------------SKKRYSPASTFKIPHTLFALDAGAVRDEFQIFRWDGVNRG---FA 105
Cdd:pfam00905   1 GSAVVLDPKTGEVLAMVGKPSYdpngfigplrnraVTSRYEPGSTFKPFTALAALDNGVLKPDETIFDWPGKQQGgksIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844   106 GHNQDQ----DLRSAMRNSTVWVYELFAKEIGDDKARRYLKKIDYGNAD----PSTSNG---DYWIEGS-------LAIS 167
Cdd:pfam00905  81 DWNQDQvgigTLRQALEYSSNWYMQKLAQKLGADKLRSYLKKFGYGNKTgiglPGENAGyltPYWLEGAtasfgigLTIT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844   168 AQEQIAFLRKLYR----------------------NELPFRVEHQRLVKDLMIVEAGRN----------WILRAKTGWEG 215
Cdd:pfam00905 161 PLQQAQAYAAIANggklvpphlvksiedkvdpkvlNKLPISKSTAEKVKDMLRLVVNDGtgtgtaavpgYKVAGKTGTAQ 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 60391844   216 RMG-------------WWVGWVEWPTGSVFFALNIDTPNRMDDLFKREAIVRAIL 257
Cdd:pfam00905 241 VAGpkgggyydgaqigWFVGYAPADNPKYAFAVLIDDPKRYYGGKVAAPIFKDIL 295
pbp2_mrdA TIGR03423
penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 ...
68-147 4.54e-05

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: 44.44  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844    68 YSPASTFKIPHTLFALDAGAVRDEFQIF---RWDGVNRGF-----AGHNqDQDLRSAMRNST-VWVYELfAKEIGDDKAR 138
Cdd:TIGR03423 304 YPPGSTFKPVVALAALEEGVITPETRIYcpgYFQLGGRRFrcwkrGGHG-RVDLRKAIEESCdVYFYQL-ALRLGIDKIA 381

                  ....*....
gi 60391844   139 RYLKKIDYG 147
Cdd:TIGR03423 382 EYAKRFGFG 390
FtsI COG0768
Cell division protein FtsI, peptidoglycan transpeptidase (Penicillin-binding protein 2) [Cell ...
68-143 1.87e-03

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: 39.42  E-value: 1.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60391844  68 YSPASTFKIPHTLFALDAGAVRDEFQI------------FR-WDGVNRGfaghnqDQDLRSAMRNST-VWVYELfAKEIG 133
Cdd:COG0768 292 YEPGSTFKPFTAAAALEEGVITPDTTFdcpgyyrvggrtIRdWDRGGHG------TLTLTEALAKSSnVGFYKL-ALRLG 364
                        90
                ....*....|
gi 60391844 134 DDKARRYLKK 143
Cdd:COG0768 365 IDKLYDYLKK 374
 
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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