LPXP_ECOLI
ID LPXP_ECOLI Reviewed; 306 AA.
AC P0ACV2; P76522; P76949;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Lipid A biosynthesis palmitoleoyltransferase {ECO:0000255|HAMAP-Rule:MF_01943, ECO:0000303|PubMed:11830594};
DE EC=2.3.1.242 {ECO:0000255|HAMAP-Rule:MF_01943, ECO:0000269|PubMed:10092655};
DE AltName: Full=Kdo(2)-lipid IV(A) palmitoleoyltransferase {ECO:0000255|HAMAP-Rule:MF_01943};
GN Name=lpxP {ECO:0000255|HAMAP-Rule:MF_01943, ECO:0000303|PubMed:10092655};
GN Synonyms=ddg; OrderedLocusNames=b2378, JW2375;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Sreekumar K.R., Schaechter M.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INDUCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=10092655; DOI=10.1074/jbc.274.14.9677;
RA Carty S.M., Sreekumar K.R., Raetz C.R.;
RT "Effect of cold shock on lipid A biosynthesis in Escherichia coli.
RT Induction at 12 degrees C of an acyltransferase specific for palmitoleoyl-
RT acyl carrier protein.";
RL J. Biol. Chem. 274:9677-9685(1999).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11830594; DOI=10.1074/jbc.m200408200;
RA Vorachek-Warren M.K., Carty S.M., Lin S., Cotter R.J., Raetz C.R.;
RT "An Escherichia coli mutant lacking the cold shock-induced
RT palmitoleoyltransferase of lipid A biosynthesis: absence of unsaturated
RT acyl chains and antibiotic hypersensitivity at 12 degrees C.";
RL J. Biol. Chem. 277:14186-14193(2002).
RN [7]
RP INDUCTION IN PERSISTER CELLS.
RC STRAIN=K12;
RX PubMed=16768798; DOI=10.1186/1471-2180-6-53;
RA Shah D., Zhang Z., Khodursky A., Kaldalu N., Kurg K., Lewis K.;
RT "Persisters: a distinct physiological state of E. coli.";
RL BMC Microbiol. 6:53-53(2006).
CC -!- FUNCTION: Catalyzes the transfer of palmitoleate from palmitoleoyl-acyl
CC carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-
CC (palmitoleoyl)-lipid IV(A). Required for the biosynthesis of a distinct
CC molecular species of lipid A, which is present only in cells grown at
CC low temperatures. It may confer a selective advantage to cells growing
CC at lower temperatures by making the outer membrane a more effective
CC barrier to harmful chemicals. {ECO:0000269|PubMed:10092655,
CC ECO:0000269|PubMed:11830594}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-[ACP] + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-
CC lipid IVA = (9Z)-hexadecenoyl-(Kdo)2-lipid IVA + holo-[ACP];
CC Xref=Rhea:RHEA:44012, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:10800,
CC ChEBI:CHEBI:60365, ChEBI:CHEBI:61520, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:83989; EC=2.3.1.242; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01943, ECO:0000269|PubMed:10092655};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01943,
CC ECO:0000269|PubMed:10092655}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01943, ECO:0000305}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01943}.
CC -!- INDUCTION: Induced more than 30-fold upon cold shock. The induced
CC activity is maximal after 2 h of cold shock, and then gradually
CC declines but does not disappear (PubMed:10092655). Induced in persister
CC cells (PubMed:16768798). {ECO:0000269|PubMed:10092655,
CC ECO:0000269|PubMed:16768798}.
CC -!- DISRUPTION PHENOTYPE: Disruption does not confer any obvious growth
CC phenotype in nutrient broth at low temperatures, but mutant shows a 10-
CC fold increase in sensitivity to rifampicin and vancomycin at 12 degrees
CC Celsius compared with wild type cells. {ECO:0000269|PubMed:11830594}.
CC -!- MISCELLANEOUS: About two-thirds of the lipid A residues of cells grown
CC at 12 degrees Celsius are acylated with palmitoleate rather than
CC laurate. {ECO:0000305|PubMed:11830594}.
CC -!- SIMILARITY: Belongs to the LpxL/LpxM/LpxP family. LpxP subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01943, ECO:0000305}.
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DR EMBL; U49787; AAB66658.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75437.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16248.1; -; Genomic_DNA.
DR RefSeq; NP_416879.4; NC_000913.3.
DR RefSeq; WP_000484404.1; NZ_STEB01000008.1.
DR AlphaFoldDB; P0ACV2; -.
DR SMR; P0ACV2; -.
DR BioGRID; 4260930; 144.
DR IntAct; P0ACV2; 6.
DR STRING; 511145.b2378; -.
DR PaxDb; P0ACV2; -.
DR PRIDE; P0ACV2; -.
DR EnsemblBacteria; AAC75437; AAC75437; b2378.
DR EnsemblBacteria; BAA16248; BAA16248; BAA16248.
DR GeneID; 66673752; -.
DR GeneID; 946847; -.
DR KEGG; ecj:JW2375; -.
DR KEGG; eco:b2378; -.
DR PATRIC; fig|1411691.4.peg.4351; -.
DR EchoBASE; EB2738; -.
DR eggNOG; COG1560; Bacteria.
DR HOGENOM; CLU_049421_1_0_6; -.
DR InParanoid; P0ACV2; -.
DR OMA; FWFHRRF; -.
DR PhylomeDB; P0ACV2; -.
DR BioCyc; EcoCyc:PALMITOTRANS-MON; -.
DR BioCyc; MetaCyc:PALMITOTRANS-MON; -.
DR BRENDA; 2.3.1.242; 2026.
DR UniPathway; UPA00030; -.
DR PRO; PR:P0ACV2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008951; F:palmitoleoyl [acyl-carrier-protein]-dependent acyltransferase activity; IDA:EcoCyc.
DR GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IMP:EcoCyc.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:InterPro.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009409; P:response to cold; IEP:EcoCyc.
DR CDD; cd07984; LPLAT_LABLAT-like; 1.
DR HAMAP; MF_01942; Lipid_A_LpxL_LpxP; 1.
DR HAMAP; MF_01943; Lipid_A_LpxP; 1.
DR InterPro; IPR004960; LipA_acyltrans.
DR InterPro; IPR011920; Lipid_A_LpxL_LpxP.
DR InterPro; IPR030857; Lipid_A_LpxP.
DR PANTHER; PTHR30606; PTHR30606; 1.
DR Pfam; PF03279; Lip_A_acyltrans; 1.
DR PIRSF; PIRSF026649; MsbB; 1.
DR TIGRFAMs; TIGR02207; lipid_A_htrB; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell inner membrane; Cell membrane;
KW Lipopolysaccharide biosynthesis; Membrane; Reference proteome;
KW Stress response; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..306
FT /note="Lipid A biosynthesis palmitoleoyltransferase"
FT /id="PRO_0000201781"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01943"
FT MOTIF 132..137
FT /note="HXXXXD motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01943"
SQ SEQUENCE 306 AA; 35493 MW; 58327F3D96C9E7B6 CRC64;
MFPQCKFSRE FLHPRYWLTW FGLGVLWLWV QLPYPVLCFL GTRIGAMARP FLKRRESIAR
KNLELCFPQH SAEEREKMIA ENFRSLGMAL VETGMAWFWP DSRVRKWFDV EGLDNLKRAQ
MQNRGVMVVG VHFMSLELGG RVMGLCQPMM ATYRPHNNQL MEWVQTRGRM RSNKAMIGRN
NLRGIVGALK KGEAVWFAPD QDYGRKGSSF APFFAVENVA TTNGTYVLSR LSGAAMLTVT
MVRKADYSGY RLFITPEMEG YPTDENQAAA YMNKIIEKEI MRAPEQYLWI HRRFKTRPVG
ESSLYI
