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Conserved domains on  [gi|447182444|ref|WP_001259700|]
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MULTISPECIES: phospholipase A [Gammaproteobacteria]

Protein Classification

phospholipase A( domain architecture ID 10793469)

outer membrane phospholipase A (OMPLA) is an integral membrane enzyme that catalyzes the hydrolysis of acylester bonds in phospholipids using calcium as a cofactor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10763 PRK10763
phospholipase A; Provisional
1-289 0e+00

phospholipase A; Provisional


:

Pssm-ID: 182708  Cd Length: 289  Bit Score: 614.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444   1 MRTLQGWLLPVFMLPMAVYAQEATVKEVHDAPAVRGSIIANMLQEHDNPFTLYPYDTNYLIYTQTSDLNKEAIASYDWAE 80
Cdd:PRK10763   1 MRTIQGWLLALLLLPLAVYAQEATVKEVHDAPAVRGSIIANMLQEHDNPFTLYPYETNYLLYTYTSDLNKEAISSYDWAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444  81 NARKDEVKFQLSLAFPLWRGILGPNSVLGASYTQKSWWQLSNSEESSPFRETNYEPQLFLGFATDYRFAGWTLRDVEMGY 160
Cdd:PRK10763  81 NARKDEVKFQLSLAFPLWRGILGDNSVLGASYTQKSWWQLSNSEESSPFRETNYEPQLFLGWATDYRFAGWTLRDVEMGY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444 161 NHDSNGRSDPTSRSWNRLYTRLMAENGNWLVEVKPWYVVGNTDDNPDITKYMGYYQLKIGYHLGDAVLSAKGQYNWNTGY 240
Cdd:PRK10763 161 NHQSNGRSDPTSRSWNRLYTRLMAQNGNWLVEVKPWYRIGSTDDNPDITKYMGYYQLKIGYHLGDAVFSAKGQYNWNTGY 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 447182444 241 GGAELGLSYPITKHVRLYTQVYSGYGESLIDYNFNQTRVGVGVMLNDLF 289
Cdd:PRK10763 241 GGAELGWSYPITKHVRFYTQVYSGYGESLIDYNFRQTRVGVGVMLNDLF 289
 
Name Accession Description Interval E-value
PRK10763 PRK10763
phospholipase A; Provisional
1-289 0e+00

phospholipase A; Provisional


Pssm-ID: 182708  Cd Length: 289  Bit Score: 614.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444   1 MRTLQGWLLPVFMLPMAVYAQEATVKEVHDAPAVRGSIIANMLQEHDNPFTLYPYDTNYLIYTQTSDLNKEAIASYDWAE 80
Cdd:PRK10763   1 MRTIQGWLLALLLLPLAVYAQEATVKEVHDAPAVRGSIIANMLQEHDNPFTLYPYETNYLLYTYTSDLNKEAISSYDWAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444  81 NARKDEVKFQLSLAFPLWRGILGPNSVLGASYTQKSWWQLSNSEESSPFRETNYEPQLFLGFATDYRFAGWTLRDVEMGY 160
Cdd:PRK10763  81 NARKDEVKFQLSLAFPLWRGILGDNSVLGASYTQKSWWQLSNSEESSPFRETNYEPQLFLGWATDYRFAGWTLRDVEMGY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444 161 NHDSNGRSDPTSRSWNRLYTRLMAENGNWLVEVKPWYVVGNTDDNPDITKYMGYYQLKIGYHLGDAVLSAKGQYNWNTGY 240
Cdd:PRK10763 161 NHQSNGRSDPTSRSWNRLYTRLMAQNGNWLVEVKPWYRIGSTDDNPDITKYMGYYQLKIGYHLGDAVFSAKGQYNWNTGY 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 447182444 241 GGAELGLSYPITKHVRLYTQVYSGYGESLIDYNFNQTRVGVGVMLNDLF 289
Cdd:PRK10763 241 GGAELGWSYPITKHVRFYTQVYSGYGESLIDYNFRQTRVGVGVMLNDLF 289
PldA COG2829
Outer membrane phospholipase A [Cell wall/membrane/envelope biogenesis];
40-287 1.09e-130

Outer membrane phospholipase A [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442077  Cd Length: 253  Bit Score: 371.12  E-value: 1.09e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444  40 ANMLQEHDNPFTLYPYDTNYLI-YTQTSDLNKEAIASYDWAENARKDEVKFQLSLAFPLWRGILGPNSVLGASYTQKSWW 118
Cdd:COG2829    1 ALERDSADNPFNLTPYKPNYFLpGTYTSNPNKEPYSPVSWAINLDNTEAKFQISFKTPLWRDLLGDNGDLYFAYTQRSFW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444 119 QLSNSEESSPFRETNYEPQLFLGFATDYRFAGWTLRDVEMGYNHDSNGRSDPTSRSWNRLYTRLMAENGNWLVEVKPWYV 198
Cdd:COG2829   81 QLYNSDDSSPFRETNYEPELFLGFPTDYKLGGWRLRGLGLGFNHQSNGRSGPLSRSWNRVYLRLGFERGNLTVSLRPWYR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444 199 VG---NTDDNPDITKYMGYYQLKIGYHLGDAVLSAKGQYNW-NTGYGGAELGLSYPITKHVRLYTQVYSGYGESLIDYNF 274
Cdd:COG2829  161 IPedaDDDDNPDIEDYMGYGDLTLGYRWGDHEFSLTLRNNLrSDNKGALQLDWSYPLSRNLRGYVQYFNGYGESLIDYNH 240
                        250
                 ....*....|...
gi 447182444 275 NQTRVGVGVMLND 287
Cdd:COG2829  241 RQTRIGIGVSLND 253
PLA1 pfam02253
Phospholipase A1; Phospholipase A1 is a bacterial outer membrane bound acyl hydrolase with a ...
44-285 6.80e-123

Phospholipase A1; Phospholipase A1 is a bacterial outer membrane bound acyl hydrolase with a broad substrate specificity EC:3.1.1.32. It has been proposed that Ser164 is the active site for Swiss:P00631.


Pssm-ID: 460509  Cd Length: 248  Bit Score: 351.10  E-value: 6.80e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444   44 QEHDNPFTLYPYDTNYLI-YTQTSDLNKEAIASYDWAENA-RKDEVKFQLSLAFPLWRGILGPNSVLGASYTQKSWWQLS 121
Cdd:pfam02253   1 QSKDNTFSLRPYKPNYLLpVTYTSSPNRDPSSPNPDNTDAeDNTEAKFQLSFKTPLAQNLFGDNGDLWFGYTQQSFWQVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444  122 NSEESSPFRETNYEPQLFLGFATDYRFAGWTLRDVEMGYNHDSNGRSDPTSRSWNRLYTRLMAENGNWLVEVKPWYVVGN 201
Cdd:pfam02253  81 NSDISRPFRETNYEPELFLVFPTDWSLLGWRLRLVGLGLNHQSNGRSGPLSRSWNRIYLMAGFERGNWAVSLKPWYRIPE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444  202 ---TDDNPDITKYMGYYQLKIGYHLGDAVLSAKGQYNWN-TGYGGAELGLSYPITKHVRLYTQVYSGYGESLIDYNFNQT 277
Cdd:pfam02253 161 sakDDDNPDIEDYMGYGELTLAYKFNDHTFSLMLRNNLRsTNKGAVELGWSFPISGNLRGYVQYFNGYGESLIDYNHRQT 240

                  ....*...
gi 447182444  278 RVGVGVML 285
Cdd:pfam02253 241 RIGLGISL 248
OMPLA cd00541
The outer membrane phospholipase A (OMPLA) is an integral membrane enzyme that catalyses the ...
50-280 2.56e-108

The outer membrane phospholipase A (OMPLA) is an integral membrane enzyme that catalyses the hydrolysis of acylester bonds in phospholipids using calcium as a cofactor. The enzyme has a fold of transmembrane beta-barrels and is widespread among Gram-negative bacteria, both in pathogens and nonpathogens. In pathogenic bacteria such as Campylobacter coli and Helicobacter pylori OMPLA is involved in pathogenesis and virulence. In nonpathogenic bacteria the physiological function of OMPLA is less clear. The Escherichia coli enzyme is involved in the secretion of bacteriocins, antibacterial peptides that are produced in order to survive under starvation conditions. The enzyme activity of OMPLA is strictly regulated to prevent uncontrolled breakdown of the surrounding phospholipids. The activity of OMPLA can be induced by membrane perturbation and concurs with dimerization of the enzyme.


Pssm-ID: 238302  Cd Length: 231  Bit Score: 313.45  E-value: 2.56e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444  50 FTLYPYDTNYLIYTQTSDLNKEAiasYDWAENARKDEVKFQLSLAFPLWRGILGPNSVLGASYTQKSWWQLSNSEESSPF 129
Cdd:cd00541    1 FLLPPYDPNYLLPSYYSPMYFLT---AYEAGNLDDTEAKFQLSFKYPLFEGLLGPNDDLYFGYTQTSLWQLYNSDDSSPF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444 130 RETNYEPQLFLGFATDYRFAGWTLRDVEMGYNHDSNGRSDPTSRSWNRLYTRLMAENGNWLVEVKPWYVVG--NTDDNPD 207
Cdd:cd00541   78 RETNYEPELFYVYPTNYKLAGGTLRMLGLGYNHESNGRSGPLSRSWNRLYLRPGWEKGNLTLGVRPWYRIPesDDDDNPD 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447182444 208 ITKYMGYYQLKIGYHLGDAVLSAKG-QYNWNTGYGGAELGLSYPITKHVRLYTQVYSGYGESLIDYNFNQTRVG 280
Cdd:cd00541  158 IADYRGYGDLKLAYGLGDHLFVLLLlRYNLRTNRGSVELDYTYPITGGLRLYVQYFNGYGESLIDYNHRQTRIG 231
 
Name Accession Description Interval E-value
PRK10763 PRK10763
phospholipase A; Provisional
1-289 0e+00

phospholipase A; Provisional


Pssm-ID: 182708  Cd Length: 289  Bit Score: 614.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444   1 MRTLQGWLLPVFMLPMAVYAQEATVKEVHDAPAVRGSIIANMLQEHDNPFTLYPYDTNYLIYTQTSDLNKEAIASYDWAE 80
Cdd:PRK10763   1 MRTIQGWLLALLLLPLAVYAQEATVKEVHDAPAVRGSIIANMLQEHDNPFTLYPYETNYLLYTYTSDLNKEAISSYDWAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444  81 NARKDEVKFQLSLAFPLWRGILGPNSVLGASYTQKSWWQLSNSEESSPFRETNYEPQLFLGFATDYRFAGWTLRDVEMGY 160
Cdd:PRK10763  81 NARKDEVKFQLSLAFPLWRGILGDNSVLGASYTQKSWWQLSNSEESSPFRETNYEPQLFLGWATDYRFAGWTLRDVEMGY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444 161 NHDSNGRSDPTSRSWNRLYTRLMAENGNWLVEVKPWYVVGNTDDNPDITKYMGYYQLKIGYHLGDAVLSAKGQYNWNTGY 240
Cdd:PRK10763 161 NHQSNGRSDPTSRSWNRLYTRLMAQNGNWLVEVKPWYRIGSTDDNPDITKYMGYYQLKIGYHLGDAVFSAKGQYNWNTGY 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 447182444 241 GGAELGLSYPITKHVRLYTQVYSGYGESLIDYNFNQTRVGVGVMLNDLF 289
Cdd:PRK10763 241 GGAELGWSYPITKHVRFYTQVYSGYGESLIDYNFRQTRVGVGVMLNDLF 289
PldA COG2829
Outer membrane phospholipase A [Cell wall/membrane/envelope biogenesis];
40-287 1.09e-130

Outer membrane phospholipase A [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442077  Cd Length: 253  Bit Score: 371.12  E-value: 1.09e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444  40 ANMLQEHDNPFTLYPYDTNYLI-YTQTSDLNKEAIASYDWAENARKDEVKFQLSLAFPLWRGILGPNSVLGASYTQKSWW 118
Cdd:COG2829    1 ALERDSADNPFNLTPYKPNYFLpGTYTSNPNKEPYSPVSWAINLDNTEAKFQISFKTPLWRDLLGDNGDLYFAYTQRSFW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444 119 QLSNSEESSPFRETNYEPQLFLGFATDYRFAGWTLRDVEMGYNHDSNGRSDPTSRSWNRLYTRLMAENGNWLVEVKPWYV 198
Cdd:COG2829   81 QLYNSDDSSPFRETNYEPELFLGFPTDYKLGGWRLRGLGLGFNHQSNGRSGPLSRSWNRVYLRLGFERGNLTVSLRPWYR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444 199 VG---NTDDNPDITKYMGYYQLKIGYHLGDAVLSAKGQYNW-NTGYGGAELGLSYPITKHVRLYTQVYSGYGESLIDYNF 274
Cdd:COG2829  161 IPedaDDDDNPDIEDYMGYGDLTLGYRWGDHEFSLTLRNNLrSDNKGALQLDWSYPLSRNLRGYVQYFNGYGESLIDYNH 240
                        250
                 ....*....|...
gi 447182444 275 NQTRVGVGVMLND 287
Cdd:COG2829  241 RQTRIGIGVSLND 253
PLA1 pfam02253
Phospholipase A1; Phospholipase A1 is a bacterial outer membrane bound acyl hydrolase with a ...
44-285 6.80e-123

Phospholipase A1; Phospholipase A1 is a bacterial outer membrane bound acyl hydrolase with a broad substrate specificity EC:3.1.1.32. It has been proposed that Ser164 is the active site for Swiss:P00631.


Pssm-ID: 460509  Cd Length: 248  Bit Score: 351.10  E-value: 6.80e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444   44 QEHDNPFTLYPYDTNYLI-YTQTSDLNKEAIASYDWAENA-RKDEVKFQLSLAFPLWRGILGPNSVLGASYTQKSWWQLS 121
Cdd:pfam02253   1 QSKDNTFSLRPYKPNYLLpVTYTSSPNRDPSSPNPDNTDAeDNTEAKFQLSFKTPLAQNLFGDNGDLWFGYTQQSFWQVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444  122 NSEESSPFRETNYEPQLFLGFATDYRFAGWTLRDVEMGYNHDSNGRSDPTSRSWNRLYTRLMAENGNWLVEVKPWYVVGN 201
Cdd:pfam02253  81 NSDISRPFRETNYEPELFLVFPTDWSLLGWRLRLVGLGLNHQSNGRSGPLSRSWNRIYLMAGFERGNWAVSLKPWYRIPE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444  202 ---TDDNPDITKYMGYYQLKIGYHLGDAVLSAKGQYNWN-TGYGGAELGLSYPITKHVRLYTQVYSGYGESLIDYNFNQT 277
Cdd:pfam02253 161 sakDDDNPDIEDYMGYGELTLAYKFNDHTFSLMLRNNLRsTNKGAVELGWSFPISGNLRGYVQYFNGYGESLIDYNHRQT 240

                  ....*...
gi 447182444  278 RVGVGVML 285
Cdd:pfam02253 241 RIGLGISL 248
OMPLA cd00541
The outer membrane phospholipase A (OMPLA) is an integral membrane enzyme that catalyses the ...
50-280 2.56e-108

The outer membrane phospholipase A (OMPLA) is an integral membrane enzyme that catalyses the hydrolysis of acylester bonds in phospholipids using calcium as a cofactor. The enzyme has a fold of transmembrane beta-barrels and is widespread among Gram-negative bacteria, both in pathogens and nonpathogens. In pathogenic bacteria such as Campylobacter coli and Helicobacter pylori OMPLA is involved in pathogenesis and virulence. In nonpathogenic bacteria the physiological function of OMPLA is less clear. The Escherichia coli enzyme is involved in the secretion of bacteriocins, antibacterial peptides that are produced in order to survive under starvation conditions. The enzyme activity of OMPLA is strictly regulated to prevent uncontrolled breakdown of the surrounding phospholipids. The activity of OMPLA can be induced by membrane perturbation and concurs with dimerization of the enzyme.


Pssm-ID: 238302  Cd Length: 231  Bit Score: 313.45  E-value: 2.56e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444  50 FTLYPYDTNYLIYTQTSDLNKEAiasYDWAENARKDEVKFQLSLAFPLWRGILGPNSVLGASYTQKSWWQLSNSEESSPF 129
Cdd:cd00541    1 FLLPPYDPNYLLPSYYSPMYFLT---AYEAGNLDDTEAKFQLSFKYPLFEGLLGPNDDLYFGYTQTSLWQLYNSDDSSPF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447182444 130 RETNYEPQLFLGFATDYRFAGWTLRDVEMGYNHDSNGRSDPTSRSWNRLYTRLMAENGNWLVEVKPWYVVG--NTDDNPD 207
Cdd:cd00541   78 RETNYEPELFYVYPTNYKLAGGTLRMLGLGYNHESNGRSGPLSRSWNRLYLRPGWEKGNLTLGVRPWYRIPesDDDDNPD 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447182444 208 ITKYMGYYQLKIGYHLGDAVLSAKG-QYNWNTGYGGAELGLSYPITKHVRLYTQVYSGYGESLIDYNFNQTRVG 280
Cdd:cd00541  158 IADYRGYGDLKLAYGLGDHLFVLLLlRYNLRTNRGSVELDYTYPITGGLRLYVQYFNGYGESLIDYNHRQTRIG 231
 
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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