LPXL_ECOLI
ID LPXL_ECOLI Reviewed; 306 AA.
AC P0ACV0; P24187;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Lipid A biosynthesis lauroyltransferase {ECO:0000255|HAMAP-Rule:MF_01942, ECO:0000303|PubMed:18656959};
DE EC=2.3.1.241 {ECO:0000255|HAMAP-Rule:MF_01942, ECO:0000269|PubMed:18656959};
DE AltName: Full=Kdo(2)-lipid IV(A) lauroyltransferase {ECO:0000255|HAMAP-Rule:MF_01942};
GN Name=lpxL {ECO:0000255|HAMAP-Rule:MF_01942, ECO:0000303|PubMed:18656959};
GN Synonyms=htrB {ECO:0000303|PubMed:1840644}, waaM;
GN OrderedLocusNames=b1054 {ECO:0000312|EMBL:AAC74138.1},
GN JW1041 {ECO:0000312|EMBL:BAA35852.1};
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=K12;
RX PubMed=1840644; DOI=10.1111/j.1365-2958.1991.tb02159.x;
RA Karow M.L., Georgopoulos C.;
RT "Sequencing, mutational analysis, and transcriptional regulation of the
RT Escherichia coli htrB gene.";
RL Mol. Microbiol. 5:2285-2292(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 200-306.
RC STRAIN=K12;
RX PubMed=1537791; DOI=10.1128/jb.174.5.1454-1461.1992;
RA Ueguchi C., Ito K.;
RT "Multicopy suppression: an approach to understanding intracellular
RT functioning of the protein export system.";
RL J. Bacteriol. 174:1454-1461(1992).
RN [6]
RP FUNCTION, AND PATHWAY.
RX PubMed=2203778; DOI=10.1016/s0021-9258(18)55412-0;
RA Brozek K.A., Raetz C.R.H.;
RT "Biosynthesis of lipid A in Escherichia coli. Acyl carrier protein-
RT dependent incorporation of laurate and myristate.";
RL J. Biol. Chem. 265:15410-15417(1990).
RN [7]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=1846149; DOI=10.1128/jb.173.2.741-750.1991;
RA Karow M., Fayet O., Cegielska A., Ziegelhoffer T., Georgopoulos C.;
RT "Isolation and characterization of the Escherichia coli htrB gene, whose
RT product is essential for bacterial viability above 33 degrees C in rich
RT media.";
RL J. Bacteriol. 173:741-750(1991).
RN [8]
RP FUNCTION, PATHWAY, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8662613; DOI=10.1074/jbc.271.20.12095;
RA Clementz T., Bednarski J.J., Raetz C.R.;
RT "Function of the htrB high temperature requirement gene of Escherchia coli
RT in the acylation of lipid A: HtrB catalyzed incorporation of laurate.";
RL J. Biol. Chem. 271:12095-12102(1996).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-132; GLU-137;
RP ARG-169; ASP-200 AND PRO-238.
RX PubMed=18656959; DOI=10.1021/bi800873n;
RA Six D.A., Carty S.M., Guan Z., Raetz C.R.;
RT "Purification and mutagenesis of LpxL, the lauroyltransferase of
RT Escherichia coli lipid A biosynthesis.";
RL Biochemistry 47:8623-8637(2008).
CC -!- FUNCTION: Catalyzes the transfer of laurate from lauroyl-acyl carrier
CC protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-(lauroyl)-lipid
CC IV(A). Has 10 fold selectivity for lauroyl-ACP over myristoyl-ACP. In
CC vitro, can also catalyze a slow second acylation reaction leading to
CC the formation of Kdo(2)-(dilauroyl)-lipid IV(A).
CC {ECO:0000269|PubMed:18656959, ECO:0000269|PubMed:2203778,
CC ECO:0000269|PubMed:8662613}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + dodecanoyl-[ACP]
CC = dodecanoyl-(Kdo)2-lipid IVA + holo-[ACP]; Xref=Rhea:RHEA:28442,
CC Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9685, ChEBI:CHEBI:60365,
CC ChEBI:CHEBI:61524, ChEBI:CHEBI:64479, ChEBI:CHEBI:65264;
CC EC=2.3.1.241; Evidence={ECO:0000255|HAMAP-Rule:MF_01942,
CC ECO:0000269|PubMed:18656959};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7 uM for lauroyl-ACP {ECO:0000269|PubMed:18656959};
CC KM=15 uM for Kdo(2)-lipid IV(A) {ECO:0000269|PubMed:18656959};
CC Vmax=95 umol/min/mg enzyme toward lauroyl-ACP
CC {ECO:0000269|PubMed:18656959};
CC Vmax=221 umol/min/mg enzyme toward Kdo(2)-lipid IV(A)
CC {ECO:0000269|PubMed:18656959};
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 3/4. {ECO:0000255|HAMAP-Rule:MF_01942, ECO:0000269|PubMed:18656959,
CC ECO:0000269|PubMed:2203778, ECO:0000269|PubMed:8662613}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01942,
CC ECO:0000269|PubMed:18656959, ECO:0000269|PubMed:2203778,
CC ECO:0000269|PubMed:8662613}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18656959}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01942, ECO:0000269|PubMed:1846149, ECO:0000269|PubMed:18656959,
CC ECO:0000269|PubMed:8662613}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01942}.
CC -!- INDUCTION: Is expressed at all temperatures, but accumulation of htrB
CC transcripts slightly declines with raising temperature. Thus, its
CC expression is not induced by heat shock. {ECO:0000269|PubMed:1840644}.
CC -!- DISRUPTION PHENOTYPE: Inactivation leads to bacterial death at
CC temperatures above 33 degrees Celsius. Phenotype at nonpermissive
CC temperatures includes an arrest of cell division followed by the
CC formation of bulges or filaments. {ECO:0000269|PubMed:1846149}.
CC -!- SIMILARITY: Belongs to the LpxL/LpxM/LpxP family. {ECO:0000255|HAMAP-
CC Rule:MF_01942, ECO:0000305}.
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DR EMBL; X61000; CAA43317.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74138.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35852.1; -; Genomic_DNA.
DR EMBL; X59939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S16888; S16888.
DR RefSeq; NP_415572.1; NC_000913.3.
DR RefSeq; WP_000183364.1; NZ_STEB01000016.1.
DR AlphaFoldDB; P0ACV0; -.
DR SMR; P0ACV0; -.
DR BioGRID; 4262842; 71.
DR IntAct; P0ACV0; 9.
DR STRING; 511145.b1054; -.
DR jPOST; P0ACV0; -.
DR PaxDb; P0ACV0; -.
DR PRIDE; P0ACV0; -.
DR EnsemblBacteria; AAC74138; AAC74138; b1054.
DR EnsemblBacteria; BAA35852; BAA35852; BAA35852.
DR GeneID; 66670679; -.
DR GeneID; 946216; -.
DR KEGG; ecj:JW1041; -.
DR KEGG; eco:b1054; -.
DR PATRIC; fig|511145.12.peg.1095; -.
DR EchoBASE; EB0459; -.
DR eggNOG; COG1560; Bacteria.
DR HOGENOM; CLU_049421_1_1_6; -.
DR InParanoid; P0ACV0; -.
DR OMA; WRIERWF; -.
DR PhylomeDB; P0ACV0; -.
DR BioCyc; EcoCyc:LAUROYLACYLTRAN-MON; -.
DR BioCyc; MetaCyc:LAUROYLACYLTRAN-MON; -.
DR BRENDA; 2.3.1.241; 2026.
DR SABIO-RK; P0ACV0; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00360; UER00485.
DR PRO; PR:P0ACV0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0016020; C:membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0008913; F:lauroyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IDA:EcoCyc.
DR GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07984; LPLAT_LABLAT-like; 1.
DR HAMAP; MF_01942; Lipid_A_LpxL_LpxP; 1.
DR InterPro; IPR004960; LipA_acyltrans.
DR InterPro; IPR011920; Lipid_A_LpxL_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; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..306
FT /note="Lipid A biosynthesis lauroyltransferase"
FT /id="PRO_0000201774"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01942"
FT MOTIF 132..137
FT /note="HXXXXD motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01942,
FT ECO:0000305|PubMed:18656959"
FT MUTAGEN 132
FT /note="H->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:18656959"
FT MUTAGEN 137
FT /note="E->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:18656959"
FT MUTAGEN 169
FT /note="R->A: 169-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:18656959"
FT MUTAGEN 200
FT /note="D->A: 14-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:18656959"
FT MUTAGEN 238
FT /note="P->A: Slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:18656959"
SQ SEQUENCE 306 AA; 35407 MW; AEA70A5EB10653B5 CRC64;
MTNLPKFSTA LLHPRYWLTW LGIGVLWLVV QLPYPVIYRL GCGLGKLALR FMKRRAKIVH
RNLELCFPEM SEQERRKMVV KNFESVGMGL METGMAWFWP DRRIARWTEV IGMEHIRDVQ
AQKRGILLVG IHFLTLELGA RQFGMQEPGI GVYRPNDNPL IDWLQTWGRL RSNKSMLDRK
DLKGMIKALK KGEVVWYAPD HDYGPRSSVF VPLFAVEQAA TTTGTWMLAR MSGACLVPFV
PRRKPDGKGY QLIMLPPECS PPLDDAETTA AWMNKVVEKC IMMAPEQYMW LHRRFKTRPE
GVPSRY
