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Conserved domains on  [gi|435286392|gb|ELO63668|]
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phospholipid:lipid A palmitoyltransferase [Salmonella enterica subsp. enterica serovar Enteritidis str. 648904 3-6]

Protein Classification

phospholipid:lipid A palmitoyltransferase( domain architecture ID 10013718)

phospholipid:lipid A palmitoyltransferase PagP catalyzes the transfer of palmitate to lipid A

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
pagP PRK11045
lipid IV(A) palmitoyltransferase PagP;
3-186 2.33e-122

lipid IV(A) palmitoyltransferase PagP;


:

Pssm-ID: 236829  Cd Length: 184  Bit Score: 342.80  E-value: 2.33e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435286392   3 IRKYFLIIALLVMPWLAIPSVSAADKGWFNTFTDNVAETWRQPEHYDLYVPAITWHARFAYDKEKTDRYNERPWGVGFGQ 82
Cdd:PRK11045   1 VKKYILILSLVFLLLLAVASACANAPSWWQTFCENVAQTWNEPEHYDLYIPAITWHNRFAYDKEKIDSYNERPWGGGFGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435286392  83 SRWDDKGNWHGLYMMAFKDSFNKWEPIGGYGWEKTWRPLEDDNFRLGLGFTAGVTARDNWNYIPIPVLLPLASIGYGPAT 162
Cdd:PRK11045  81 SRYDEKGNWHGLYAMAFKDSHNKWEPIAGYGWEKTWRPLADENFRLGLGFTAGVTARDDWNYIPIPGLLPLASIGYGRLT 160
                        170       180
                 ....*....|....*....|....
gi 435286392 163 FQMTYIPGSYNNGNVYFAWMRFQF 186
Cdd:PRK11045 161 FQMTYIPGTYNNGNVLFAWMRFQF 184
 
Name Accession Description Interval E-value
pagP PRK11045
lipid IV(A) palmitoyltransferase PagP;
3-186 2.33e-122

lipid IV(A) palmitoyltransferase PagP;


Pssm-ID: 236829  Cd Length: 184  Bit Score: 342.80  E-value: 2.33e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435286392   3 IRKYFLIIALLVMPWLAIPSVSAADKGWFNTFTDNVAETWRQPEHYDLYVPAITWHARFAYDKEKTDRYNERPWGVGFGQ 82
Cdd:PRK11045   1 VKKYILILSLVFLLLLAVASACANAPSWWQTFCENVAQTWNEPEHYDLYIPAITWHNRFAYDKEKIDSYNERPWGGGFGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435286392  83 SRWDDKGNWHGLYMMAFKDSFNKWEPIGGYGWEKTWRPLEDDNFRLGLGFTAGVTARDNWNYIPIPVLLPLASIGYGPAT 162
Cdd:PRK11045  81 SRYDEKGNWHGLYAMAFKDSHNKWEPIAGYGWEKTWRPLADENFRLGLGFTAGVTARDDWNYIPIPGLLPLASIGYGRLT 160
                        170       180
                 ....*....|....*....|....
gi 435286392 163 FQMTYIPGSYNNGNVYFAWMRFQF 186
Cdd:PRK11045 161 FQMTYIPGTYNNGNVLFAWMRFQF 184
PagP pfam07017
Antimicrobial peptide resistance and lipid A acylation protein PagP; This family consists of ...
37-183 5.30e-89

Antimicrobial peptide resistance and lipid A acylation protein PagP; This family consists of several bacterial antimicrobial peptide resistance and lipid A acylation (PagP) proteins. The bacterial outer membrane enzyme PagP transfers a palmitate chain from a phospholipid to lipid A. In a number of pathogenic Gram-negative bacteria, PagP confers resistance to certain cationic antimicrobial peptides produced during the host innate immune response.


Pssm-ID: 429249  Cd Length: 144  Bit Score: 256.83  E-value: 5.30e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435286392   37 NVAETWRQPEHyDLYVPAITWHARFAYDKEKTDRYNERPWGVGFGQSRWDDKGNWHGLYMMAFKDSFNKWEPIGGYGWEK 116
Cdd:pfam07017   1 RVSQTWNQGQY-DLYLPGYTWHNRFTYDKEKIDSYNERPWGLGYGKSRYDEDGNWHGLYAMAFKDSHNKWEPIAGYGYQK 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 435286392  117 TWRPleDDNFRLGLGFTAGVTARDNWNYIPIPVLLPLASIGYGPATFQMTYIPGSYNNGNVYFAWMR 183
Cdd:pfam07017  80 MWRP--AEDFHLGLGYTAGVTSRDDYHYIPFPGILPLASIGYKRLTLQATYIPGGYNNGNVLFAWGR 144
 
Name Accession Description Interval E-value
pagP PRK11045
lipid IV(A) palmitoyltransferase PagP;
3-186 2.33e-122

lipid IV(A) palmitoyltransferase PagP;


Pssm-ID: 236829  Cd Length: 184  Bit Score: 342.80  E-value: 2.33e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435286392   3 IRKYFLIIALLVMPWLAIPSVSAADKGWFNTFTDNVAETWRQPEHYDLYVPAITWHARFAYDKEKTDRYNERPWGVGFGQ 82
Cdd:PRK11045   1 VKKYILILSLVFLLLLAVASACANAPSWWQTFCENVAQTWNEPEHYDLYIPAITWHNRFAYDKEKIDSYNERPWGGGFGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435286392  83 SRWDDKGNWHGLYMMAFKDSFNKWEPIGGYGWEKTWRPLEDDNFRLGLGFTAGVTARDNWNYIPIPVLLPLASIGYGPAT 162
Cdd:PRK11045  81 SRYDEKGNWHGLYAMAFKDSHNKWEPIAGYGWEKTWRPLADENFRLGLGFTAGVTARDDWNYIPIPGLLPLASIGYGRLT 160
                        170       180
                 ....*....|....*....|....
gi 435286392 163 FQMTYIPGSYNNGNVYFAWMRFQF 186
Cdd:PRK11045 161 FQMTYIPGTYNNGNVLFAWMRFQF 184
PagP pfam07017
Antimicrobial peptide resistance and lipid A acylation protein PagP; This family consists of ...
37-183 5.30e-89

Antimicrobial peptide resistance and lipid A acylation protein PagP; This family consists of several bacterial antimicrobial peptide resistance and lipid A acylation (PagP) proteins. The bacterial outer membrane enzyme PagP transfers a palmitate chain from a phospholipid to lipid A. In a number of pathogenic Gram-negative bacteria, PagP confers resistance to certain cationic antimicrobial peptides produced during the host innate immune response.


Pssm-ID: 429249  Cd Length: 144  Bit Score: 256.83  E-value: 5.30e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 435286392   37 NVAETWRQPEHyDLYVPAITWHARFAYDKEKTDRYNERPWGVGFGQSRWDDKGNWHGLYMMAFKDSFNKWEPIGGYGWEK 116
Cdd:pfam07017   1 RVSQTWNQGQY-DLYLPGYTWHNRFTYDKEKIDSYNERPWGLGYGKSRYDEDGNWHGLYAMAFKDSHNKWEPIAGYGYQK 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 435286392  117 TWRPleDDNFRLGLGFTAGVTARDNWNYIPIPVLLPLASIGYGPATFQMTYIPGSYNNGNVYFAWMR 183
Cdd:pfam07017  80 MWRP--AEDFHLGLGYTAGVTSRDDYHYIPFPGILPLASIGYKRLTLQATYIPGGYNNGNVLFAWGR 144
 
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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