LPXM_ECOLI
ID LPXM_ECOLI Reviewed; 323 AA.
AC P24205;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Lipid A biosynthesis myristoyltransferase {ECO:0000255|HAMAP-Rule:MF_01944, ECO:0000305};
DE EC=2.3.1.243 {ECO:0000255|HAMAP-Rule:MF_01944, ECO:0000269|PubMed:9099672, ECO:0000305|PubMed:10092655};
DE AltName: Full=Kdo(2)-lauroyl-lipid IV(A) myristoyltransferase {ECO:0000255|HAMAP-Rule:MF_01944};
GN Name=lpxM {ECO:0000255|HAMAP-Rule:MF_01944, ECO:0000303|PubMed:10092655};
GN Synonyms=msbB {ECO:0000303|PubMed:1732206};
GN OrderedLocusNames=b1855, JW1844;
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;
RX PubMed=1732206; DOI=10.1128/jb.174.3.702-710.1992;
RA Karow M.L., Georgopoulos C.;
RT "Isolation and characterization of the Escherichia coli msbB gene, a
RT multicopy suppressor of null mutations in the high-temperature requirement
RT gene htrB.";
RL J. Bacteriol. 174:702-710(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1356966; DOI=10.1128/jb.174.20.6394-6403.1992;
RA Engel H., Smink A.J., van Wijngaarden L., Keck W.;
RT "Murein-metabolizing enzymes from Escherichia coli: existence of a second
RT lytic transglycosylase.";
RL J. Bacteriol. 174:6394-6403(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=9099672; DOI=10.1074/jbc.272.16.10353;
RA Clementz T., Zhou Z., Raetz C.R.H.;
RT "Function of the Escherichia coli msbB gene, a multicopy suppressor of htrB
RT knockouts, in the acylation of lipid A. Acylation by MsbB follows laurate
RT incorporation by HtrB.";
RL J. Biol. Chem. 272:10353-10360(1997).
RN [7]
RP CATALYTIC ACTIVITY, PATHWAY, AND GENE NAME.
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 [8]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16467300; DOI=10.1074/jbc.m600435200;
RA Wang X., McGrath S.C., Cotter R.J., Raetz C.R.;
RT "Expression cloning and periplasmic orientation of the Francisella novicida
RT lipid A 4'-phosphatase LpxF.";
RL J. Biol. Chem. 281:9321-9330(2006).
CC -!- FUNCTION: Catalyzes the transfer of myristate from myristoyl-acyl
CC carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)-
CC lipid A. Can probably also catalyze the transfer of myristate to
CC Kdo(2)-(palmitoleoyl)-lipid IV(A) to form the cold-adapted Kdo(2)-lipid
CC A. In vitro, can acylate Kdo(2)-lipid IV(A), but acylation of (KDO)2-
CC (lauroyl)-lipid IV(A) is about 100 times faster. In vitro, can use
CC lauroyl-ACP but displays a slight kinetic preference for myristoyl-ACP.
CC {ECO:0000269|PubMed:9099672, ECO:0000305|PubMed:10092655}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-(Kdo)2-lipid IVA + tetradecanoyl-[ACP] = alpha-Kdo-
CC (2->4)-alpha-Kdo-(2->6)-lipid A + holo-[ACP]; Xref=Rhea:RHEA:28438,
CC Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:58540,
CC ChEBI:CHEBI:61524, ChEBI:CHEBI:64479, ChEBI:CHEBI:78477;
CC EC=2.3.1.243; Evidence={ECO:0000255|HAMAP-Rule:MF_01944,
CC ECO:0000269|PubMed:9099672};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-(Kdo)2-lipid IVA + tetradecanoyl-[ACP] =
CC ((9Z)-hexadecenoyl-tetradecanoyl)-(Kdo)2-lipid A + holo-[ACP];
CC Xref=Rhea:RHEA:28434, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:61520, ChEBI:CHEBI:61522, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78477; Evidence={ECO:0000305|PubMed:10092655};
CC -!- PATHWAY: Glycolipid biosynthesis; KDO(2)-lipid A biosynthesis; KDO(2)-
CC lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid IV(A): step
CC 4/4. {ECO:0000255|HAMAP-Rule:MF_01944, ECO:0000269|PubMed:9099672,
CC ECO:0000305|PubMed:10092655}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01944,
CC ECO:0000269|PubMed:9099672, ECO:0000305|PubMed:10092655}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01944, ECO:0000269|PubMed:9099672}; Single-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01944}.
CC -!- DISRUPTION PHENOTYPE: Makes pentaacylated lipid A rather than the usual
CC hexaacylated lipid A. {ECO:0000269|PubMed:16467300}.
CC -!- SIMILARITY: Belongs to the LpxL/LpxM/LpxP family. LpxM subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01944, ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the membrane-bound lytic murein
CC transglycosylase (MLT). {ECO:0000305|PubMed:1356966}.
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DR EMBL; M77039; AAA24181.1; -; Genomic_DNA.
DR EMBL; M87660; AAA96706.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74925.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15663.1; -; Genomic_DNA.
DR PIR; A42608; A42608.
DR RefSeq; NP_416369.1; NC_000913.3.
DR RefSeq; WP_000448381.1; NZ_STEB01000009.1.
DR AlphaFoldDB; P24205; -.
DR SMR; P24205; -.
DR BioGRID; 4260351; 239.
DR DIP; DIP-10262N; -.
DR IntAct; P24205; 21.
DR STRING; 511145.b1855; -.
DR jPOST; P24205; -.
DR PaxDb; P24205; -.
DR PRIDE; P24205; -.
DR EnsemblBacteria; AAC74925; AAC74925; b1855.
DR EnsemblBacteria; BAA15663; BAA15663; BAA15663.
DR GeneID; 66674255; -.
DR GeneID; 945143; -.
DR KEGG; ecj:JW1844; -.
DR KEGG; eco:b1855; -.
DR PATRIC; fig|511145.12.peg.1934; -.
DR EchoBASE; EB0609; -.
DR eggNOG; COG1560; Bacteria.
DR HOGENOM; CLU_049421_1_0_6; -.
DR InParanoid; P24205; -.
DR OMA; QMFATAP; -.
DR PhylomeDB; P24205; -.
DR BioCyc; EcoCyc:MYRISTOYLACYLTRAN-MON; -.
DR BioCyc; MetaCyc:MYRISTOYLACYLTRAN-MON; -.
DR BRENDA; 2.3.1.243; 2026.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00360; UER00486.
DR PRO; PR:P24205; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:EcoCyc.
DR GO; GO:0019107; F:myristoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IDA:EcoCyc.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07984; LPLAT_LABLAT-like; 1.
DR HAMAP; MF_01944; Lipid_A_LpxM; 1.
DR InterPro; IPR004960; LipA_acyltrans.
DR InterPro; IPR011921; Lipid_A_MsbB.
DR PANTHER; PTHR30606; PTHR30606; 1.
DR Pfam; PF03279; Lip_A_acyltrans; 1.
DR PIRSF; PIRSF026649; MsbB; 1.
DR TIGRFAMs; TIGR02208; lipid_A_msbB; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell inner membrane; Cell membrane;
KW Lipopolysaccharide biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..323
FT /note="Lipid A biosynthesis myristoyltransferase"
FT /id="PRO_0000201777"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01944"
FT MOTIF 139..144
FT /note="HXXXXD motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01944, ECO:0000305"
SQ SEQUENCE 323 AA; 37410 MW; 94DAF38A757D20CD CRC64;
METKKNNSEY IPEFDKSFRH PRYWGAWLGV AAMAGIALTP PKFRDPILAR LGRFAGRLGK
SSRRRALINL SLCFPERSEA EREAIVDEMF ATAPQAMAMM AELAIRGPEK IQPRVDWQGL
EIIEEMRRNN EKVIFLVPHG WAVDIPAMLM ASQGQKMAAM FHNQGNPVFD YVWNTVRRRF
GGRLHARNDG IKPFIQSVRQ GYWGYYLPDQ DHGPEHSEFV DFFATYKATL PAIGRLMKVC
RARVVPLFPI YDGKTHRLTI QVRPPMDDLL EADDHTIARR MNEEVEIFVG PRPEQYTWIL
KLLKTRKPGE IQPYKRKDLY PIK
