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Conserved domains on  [gi|15600707|ref|NP_254201|]
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beta-lactamase [Pseudomonas aeruginosa PAO1]

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];
14-262 1.12e-134

Beta-lactamase class D [Defense mechanisms];


:

Pssm-ID: 442014 [Multi-domain]  Cd Length: 267  Bit Score: 380.38  E-value: 1.12e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707  14 GHTQASEWNDSQAVDKLFGAAGVKGTFVLYDVQRQRYVGHDRERAETRFVPASTYKVANSLIGLSTGAVRSADEVLPYGG 93
Cdd:COG2602  20 AAAAAANVIERPDLAKLFDEAGVEGTFVLYDLKTGKYIVYNKERAETRFSPASTFKIPNSLIALETGVIKDENEVFKWDG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707  94 KPQRFKAWEHDMSLRDAIKASNVPVYQELARRIGLERMRANVSRLGYGNAEIGQVVDNFWLVGPLKISAMEQTRFLLRLA 173
Cdd:COG2602 100 VKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKYLDKLNYGNADISGGIDTFWLDGSLKISALEQIDFLKRLY 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707 174 QGELPFPAPVQSTVRAMTLLESGPGWELHGKTGWCFDCTPELGWWVGWVKRNERLYGFALNIDMPgGEADIGKRVELGKA 253
Cdd:COG2602 180 RNKLPFSKRTQDIVKDIMIVEKTPNYTLYGKTGWGFRDDPDIGWFVGWVEKNDNVYFFATNIDIP-DEADLPKRKEITRK 258

                ....*....
gi 15600707 254 SLKALGILP 262
Cdd:COG2602 259 ILKQLGLLP 267
 
Name Accession Description Interval E-value
YbxI COG2602
Beta-lactamase class D [Defense mechanisms];
14-262 1.12e-134

Beta-lactamase class D [Defense mechanisms];


Pssm-ID: 442014 [Multi-domain]  Cd Length: 267  Bit Score: 380.38  E-value: 1.12e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707  14 GHTQASEWNDSQAVDKLFGAAGVKGTFVLYDVQRQRYVGHDRERAETRFVPASTYKVANSLIGLSTGAVRSADEVLPYGG 93
Cdd:COG2602  20 AAAAAANVIERPDLAKLFDEAGVEGTFVLYDLKTGKYIVYNKERAETRFSPASTFKIPNSLIALETGVIKDENEVFKWDG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707  94 KPQRFKAWEHDMSLRDAIKASNVPVYQELARRIGLERMRANVSRLGYGNAEIGQVVDNFWLVGPLKISAMEQTRFLLRLA 173
Cdd:COG2602 100 VKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKYLDKLNYGNADISGGIDTFWLDGSLKISALEQIDFLKRLY 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707 174 QGELPFPAPVQSTVRAMTLLESGPGWELHGKTGWCFDCTPELGWWVGWVKRNERLYGFALNIDMPgGEADIGKRVELGKA 253
Cdd:COG2602 180 RNKLPFSKRTQDIVKDIMIVEKTPNYTLYGKTGWGFRDDPDIGWFVGWVEKNDNVYFFATNIDIP-DEADLPKRKEITRK 258

                ....*....
gi 15600707 254 SLKALGILP 262
Cdd:COG2602 259 ILKQLGLLP 267
Transpeptidase pfam00905
Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss: ...
38-256 1.01e-33

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: 123.68  E-value: 1.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707    38 GTFVLYD---------VQRQRY-----VGHDRERA-ETRFVPASTYKVANSLIGLSTGAVrSADEVLPYGGK----PQRF 98
Cdd:pfam00905   1 GSAVVLDpktgevlamVGKPSYdpngfIGPLRNRAvTSRYEPGSTFKPFTALAALDNGVL-KPDETIFDWPGkqqgGKSI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707    99 KAWEHDM----SLRDAIKASNVPVYQELARRIGLERMRANVSRLGYGNA-------EIGQVVDNFWLVGP-------LKI 160
Cdd:pfam00905  80 GDWNQDQvgigTLRQALEYSSNWYMQKLAQKLGADKLRSYLKKFGYGNKtgiglpgENAGYLTPYWLEGAtasfgigLTI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707   161 SAMEQTRFLLRLAQG----------------------ELPFPAPVQSTVRAM----------TLLESGPGWELHGKTGW- 207
Cdd:pfam00905 160 TPLQQAQAYAAIANGgklvpphlvksiedkvdpkvlnKLPISKSTAEKVKDMlrlvvndgtgTGTAAVPGYKVAGKTGTa 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15600707   208 --------CFDCTPELGWWVGWVKRNERLYGFALNIDMPGGEADIGKRVELGKASLK 256
Cdd:pfam00905 240 qvagpkggGYYDGAQIGWFVGYAPADNPKYAFAVLIDDPKRYYGGKVAAPIFKDILE 296
pbp2_mrdA TIGR03423
penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 ...
64-141 9.78e-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: 49.44  E-value: 9.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707    64 PASTYKVANSLIGLSTGaVRSADEVLP------YGGKPQR-FKAWEH-DMSLRDAIKAS-NVPVYQeLARRIGLERMRAN 134
Cdd:TIGR03423 306 PGSTFKPVVALAALEEG-VITPETRIYcpgyfqLGGRRFRcWKRGGHgRVDLRKAIEEScDVYFYQ-LALRLGIDKIAEY 383

                  ....*..
gi 15600707   135 VSRLGYG 141
Cdd:TIGR03423 384 AKRFGFG 390
 
Name Accession Description Interval E-value
YbxI COG2602
Beta-lactamase class D [Defense mechanisms];
14-262 1.12e-134

Beta-lactamase class D [Defense mechanisms];


Pssm-ID: 442014 [Multi-domain]  Cd Length: 267  Bit Score: 380.38  E-value: 1.12e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707  14 GHTQASEWNDSQAVDKLFGAAGVKGTFVLYDVQRQRYVGHDRERAETRFVPASTYKVANSLIGLSTGAVRSADEVLPYGG 93
Cdd:COG2602  20 AAAAAANVIERPDLAKLFDEAGVEGTFVLYDLKTGKYIVYNKERAETRFSPASTFKIPNSLIALETGVIKDENEVFKWDG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707  94 KPQRFKAWEHDMSLRDAIKASNVPVYQELARRIGLERMRANVSRLGYGNAEIGQVVDNFWLVGPLKISAMEQTRFLLRLA 173
Cdd:COG2602 100 VKRPFPAWNRDMTLRSAFKVSAVWYYQELARRIGKERMQKYLDKLNYGNADISGGIDTFWLDGSLKISALEQIDFLKRLY 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707 174 QGELPFPAPVQSTVRAMTLLESGPGWELHGKTGWCFDCTPELGWWVGWVKRNERLYGFALNIDMPgGEADIGKRVELGKA 253
Cdd:COG2602 180 RNKLPFSKRTQDIVKDIMIVEKTPNYTLYGKTGWGFRDDPDIGWFVGWVEKNDNVYFFATNIDIP-DEADLPKRKEITRK 258

                ....*....
gi 15600707 254 SLKALGILP 262
Cdd:COG2602 259 ILKQLGLLP 267
Transpeptidase pfam00905
Penicillin binding protein transpeptidase domain; The active site serine (residue 337 in Swiss: ...
38-256 1.01e-33

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: 123.68  E-value: 1.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707    38 GTFVLYD---------VQRQRY-----VGHDRERA-ETRFVPASTYKVANSLIGLSTGAVrSADEVLPYGGK----PQRF 98
Cdd:pfam00905   1 GSAVVLDpktgevlamVGKPSYdpngfIGPLRNRAvTSRYEPGSTFKPFTALAALDNGVL-KPDETIFDWPGkqqgGKSI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707    99 KAWEHDM----SLRDAIKASNVPVYQELARRIGLERMRANVSRLGYGNA-------EIGQVVDNFWLVGP-------LKI 160
Cdd:pfam00905  80 GDWNQDQvgigTLRQALEYSSNWYMQKLAQKLGADKLRSYLKKFGYGNKtgiglpgENAGYLTPYWLEGAtasfgigLTI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707   161 SAMEQTRFLLRLAQG----------------------ELPFPAPVQSTVRAM----------TLLESGPGWELHGKTGW- 207
Cdd:pfam00905 160 TPLQQAQAYAAIANGgklvpphlvksiedkvdpkvlnKLPISKSTAEKVKDMlrlvvndgtgTGTAAVPGYKVAGKTGTa 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15600707   208 --------CFDCTPELGWWVGWVKRNERLYGFALNIDMPGGEADIGKRVELGKASLK 256
Cdd:pfam00905 240 qvagpkggGYYDGAQIGWFVGYAPADNPKYAFAVLIDDPKRYYGGKVAAPIFKDILE 296
PenP COG2367
Beta-lactamase class A [Defense mechanisms];
25-207 3.83e-09

Beta-lactamase class A [Defense mechanisms];


Pssm-ID: 441934 [Multi-domain]  Cd Length: 276  Bit Score: 56.06  E-value: 3.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707  25 QAVDKLFGAAGVKGTFVLYDVQRQRYVGHdreRAETRFVPASTYK----------VANSLIGLSTGAVRSADEVLPYGGK 94
Cdd:COG2367  22 AELAALEAALGGRVGVYVLDLDTGETVGI---NADERFPAASTFKlpvlaavlrqVDAGKLSLDERVTLTPEDLVGGSGI 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707  95 PQRFKAwEHDMSLRDAIK---------ASNVpvyqeLARRIGLERMRANVSRLGYGNAEIGQVVD--NFWLVGPL-KISA 162
Cdd:COG2367  99 LQKLPD-GTGLTLRELAElmitvsdntATNL-----LLRLLGPDAVNAFLRSLGLTDTRLDRKEPdlNELPGDGRnTTTP 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15600707 163 MEQTRFLLRLAQGELpFPAPVQSTVRAM-------TLLESG--PGWELHGKTGW 207
Cdd:COG2367 173 RDMARLLAALYRGEL-LSPESRARLLDWlarqtgrDRLRAGlpEGWRVAHKTGT 225
FtsI COG0768
Cell division protein FtsI, peptidoglycan transpeptidase (Penicillin-binding protein 2) [Cell ...
62-141 8.74e-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: 52.52  E-value: 8.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707  62 FVPASTYKVANSLIGLSTGAVRSADEV-----LPYGGkpQRFKAWEH----DMSLRDAI-KASNVPVYQeLARRIGLERM 131
Cdd:COG0768 292 YEPGSTFKPFTAAAALEEGVITPDTTFdcpgyYRVGG--RTIRDWDRgghgTLTLTEALaKSSNVGFYK-LALRLGIDKL 368
                        90
                ....*....|
gi 15600707 132 RANVSRLGYG 141
Cdd:COG0768 369 YDYLKKFGLG 378
pbp2_mrdA TIGR03423
penicillin-binding protein 2; Members of this protein family are penicillin-binding protein 2 ...
64-141 9.78e-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: 49.44  E-value: 9.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707    64 PASTYKVANSLIGLSTGaVRSADEVLP------YGGKPQR-FKAWEH-DMSLRDAIKAS-NVPVYQeLARRIGLERMRAN 134
Cdd:TIGR03423 306 PGSTFKPVVALAALEEG-VITPETRIYcpgyfqLGGRRFRcWKRGGHgRVDLRKAIEEScDVYFYQ-LALRLGIDKIAEY 383

                  ....*..
gi 15600707   135 VSRLGYG 141
Cdd:TIGR03423 384 AKRFGFG 390
Beta-lactamase2 pfam13354
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ...
40-208 5.01e-06

Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is closely related to Beta-lactamase, pfam00144, the serine beta-lactamase-like superfamily, which contains the distantly related pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.


Pssm-ID: 463854 [Multi-domain]  Cd Length: 215  Bit Score: 46.11  E-value: 5.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707    40 FVLYDVQRQRYVGHdreRAETRFVPASTYKVANSL----------IGLSTGAVRSADEVLPYGGKPQRFKAWeHDMSLRD 109
Cdd:pfam13354   2 IYVRDLDTGEELGI---NGDRSFPAASTIKVPILLavleqvdegkLSLDERLTVTAEDKVGGSGILQYLPDG-SQLSLRD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600707   110 AIK---------ASNVpvyqeLARRIGLERMRANVSRLGYGNAEIGQVVDNFWLVGPL---KISAMEQTRFLLRLAQGEL 177
Cdd:pfam13354  78 LLTlmiavsdntATNL-----LIDRLGLEAVNARLRALGLRDTRLRRKLPDLRAADKGgtnTTTARDMAKLLEALYRGEL 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 15600707   178 pfpAPVQSTVRAMTLLES-----------GPGWELHGKTGWC 208
Cdd:pfam13354 153 ---LSPESTDRLLDILSRqqfrdrlpaglPKGARVAHKTGDL 191
 
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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