Lipid A palmitoyltransferase PagP
Details
- Name
- Lipid A palmitoyltransferase PagP
- Synonyms
- 2.3.1.-
- Antimicrobial peptide resistance
- crcA
- Lipid A acylation protein
- ybeG
- Gene Name
- pagP
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011416|Lipid A palmitoyltransferase PagP MNVSKYVAIFSFVFIQLISVGKVFANADEWMTTFRENIAQTWQQPEHYDLYIPAITWHAR FAYDKEKTDRYNERPWGGGFGLSRWDEKGNWHGLYAMAFKDSWNKWEPIAGYGWESTWRP LADENFHLGLGFTAGVTARDNWNYIPLPVLLPLASVGYGPVTFQMTYIPGTYNNGNVYFA WMRFQF
- Number of residues
- 186
- Molecular Weight
- 21769.475
- Theoretical pI
- 6.52
- GO Classification
- FunctionsO-palmitoyltransferase activityProcesseslipid A biosynthetic processComponentscell outer membrane / integral component of membrane
- General Function
- O-palmitoyltransferase activity
- Specific Function
- PagP is required both for biosynthesis of hepta-acylated lipid A species containing palmitate and for resistance to cationic antimicrobial peptides (CAMPs). It catalyzes the transfer of a palmitate chain (16:0) from the sn-1 position of a glycerophospholipid to the free hydroxyl group of the (R)-3-hydroxymyristate chain at position 2 of lipid A (endotoxin). Modifications of lipid A with a palmitate chain allow to evade host immune defenses by resisting antimicrobial peptides and attenuating the inflammatory response to infection triggered by lipopolysaccharide through the Toll-like receptor 4 (TLR4) signal transduction pathway. Phosphatidylglycerol (PtdGro), phosphatidylethanolamine (PtdEtn), phosphatidylserine (PtdSer) and phosphatidic acid (Ptd-OH) are all effective acyl donors.
- Pfam Domain Function
- PagP (PF07017)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cell outer membrane
- Gene sequence
>lcl|BSEQ0011417|Lipid A palmitoyltransferase PagP (pagP) ATGAACGTGAGTAAATATGTCGCTATCTTTTCCTTTGTTTTTATTCAGTTAATCAGCGTT GGTAAAGTTTTTGCTAACGCAGATGAGTGGATGACAACGTTTAGAGAAAATATTGCACAA ACCTGGCAACAGCCTGAACATTATGATTTATATATTCCTGCCATCACCTGGCATGCACGT TTCGCTTACGACAAAGAAAAAACCGATCGCTATAACGAGCGACCGTGGGGTGGCGGTTTT GGCCTGTCGCGTTGGGATGAAAAAGGAAACTGGCATGGCCTGTATGCCATGGCATTTAAG GACTCGTGGAACAAATGGGAACCGATTGCCGGATACGGATGGGAAAGTACCTGGCGACCG CTGGCGGATGAAAATTTTCATTTAGGTCTGGGATTCACCGCTGGCGTAACGGCACGCGAT AACTGGAATTACATCCCTCTCCCGGTTCTACTGCCATTGGCCTCCGTGGGTTATGGCCCA GTGACTTTTCAGATGACCTACATTCCGGGTACCTACAACAATGGCAATGTGTACTTTGCC TGGATGCGCTTTCAGTTTTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P37001 UniProtKB Entry Name PAGP_ECOLI GenBank Protein ID 26986711 GenBank Gene ID S83396 - General References
- Hu KH, Liu E, Dean K, Gingras M, DeGraff W, Trun NJ: Overproduction of three genes leads to camphor resistance and chromosome condensation in Escherichia coli. Genetics. 1996 Aug;143(4):1521-32. [Article]
- Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Bishop RE, Gibbons HS, Guina T, Trent MS, Miller SI, Raetz CR: Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria. EMBO J. 2000 Oct 2;19(19):5071-80. [Article]
- Guo L, Lim KB, Poduje CM, Daniel M, Gunn JS, Hackett M, Miller SI: Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides. Cell. 1998 Oct 16;95(2):189-98. [Article]
- Khan MA, Moktar J, Mott PJ, Vu M, McKie AH, Pinter T, Hof F, Bishop RE: Inscribing the perimeter of the PagP hydrocarbon ruler by site-specific chemical alkylation. Biochemistry. 2010 Oct 26;49(42):9046-57. doi: 10.1021/bi1011496. [Article]
- Hwang PM, Choy WY, Lo EI, Chen L, Forman-Kay JD, Raetz CR, Prive GG, Bishop RE, Kay LE: Solution structure and dynamics of the outer membrane enzyme PagP by NMR. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13560-5. Epub 2002 Sep 30. [Article]
- Ahn VE, Lo EI, Engel CK, Chen L, Hwang PM, Kay LE, Bishop RE, Prive GG: A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin. EMBO J. 2004 Aug 4;23(15):2931-41. Epub 2004 Jul 22. [Article]
- Cuesta-Seijo JA, Neale C, Khan MA, Moktar J, Tran CD, Bishop RE, Pomes R, Prive GG: PagP crystallized from SDS/cosolvent reveals the route for phospholipid access to the hydrocarbon ruler. Structure. 2010 Sep 8;18(9):1210-9. doi: 10.1016/j.str.2010.06.014. [Article]