LPXL_HAEIN
ID LPXL_HAEIN Reviewed; 311 AA.
AC P45239; Q48045;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Lipid A biosynthesis lauroyltransferase {ECO:0000255|HAMAP-Rule:MF_01942};
DE EC=2.3.1.241 {ECO:0000255|HAMAP-Rule:MF_01942};
DE AltName: Full=Kdo(2)-lipid IV(A) lauroyltransferase {ECO:0000255|HAMAP-Rule:MF_01942};
GN Name=lpxL {ECO:0000255|HAMAP-Rule:MF_01942}; Synonyms=htrB, waaM;
GN OrderedLocusNames=HI_1527;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NTHi 2019;
RX PubMed=7592970; DOI=10.1074/jbc.270.45.27151;
RA Lee N.-G., Sunshine M.G., Engstrom J.J., Gibson B.W., Apicella M.A.;
RT "Mutation of the htrB locus of Haemophilus influenzae nontypable strain
RT 2019 is associated with modifications of lipid A and phosphorylation of the
RT lipo-oligosaccharide.";
RL J. Biol. Chem. 270:27151-27159(1995).
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). {ECO:0000255|HAMAP-Rule:MF_01942}.
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 -!- 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}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01942}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01942}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01942}.
CC -!- SIMILARITY: Belongs to the LpxL/LpxM/LpxP family. {ECO:0000255|HAMAP-
CC Rule:MF_01942}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23173.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L42023; AAC23173.1; ALT_INIT; Genomic_DNA.
DR EMBL; U17642; AAC43515.1; -; Genomic_DNA.
DR PIR; D64127; D64127.
DR RefSeq; NP_439676.2; NC_000907.1.
DR RefSeq; WP_005693550.1; NC_000907.1.
DR AlphaFoldDB; P45239; -.
DR SMR; P45239; -.
DR STRING; 71421.HI_1527; -.
DR EnsemblBacteria; AAC23173; AAC23173; HI_1527.
DR KEGG; hin:HI_1527; -.
DR PATRIC; fig|71421.8.peg.1598; -.
DR eggNOG; COG1560; Bacteria.
DR HOGENOM; CLU_049421_1_1_6; -.
DR PhylomeDB; P45239; -.
DR BioCyc; HINF71421:G1GJ1-1549-MON; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00360; UER00485.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008913; F:lauroyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:InterPro.
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 3: Inferred from homology;
KW Acyltransferase; Cell inner membrane; Cell membrane;
KW Lipopolysaccharide biosynthesis; Membrane; Reference proteome;
KW Stress response; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..311
FT /note="Lipid A biosynthesis lauroyltransferase"
FT /id="PRO_0000201776"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01942"
FT MOTIF 134..139
FT /note="HXXXXD motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01942"
FT CONFLICT 57
FT /note="E -> K (in Ref. 2; AAC43515)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="V -> T (in Ref. 2; AAC43515)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="T -> V (in Ref. 2; AAC43515)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="A -> V (in Ref. 2; AAC43515)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..290
FT /note="DITI -> GISQ (in Ref. 2; AAC43515)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="K -> N (in Ref. 2; AAC43515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 36152 MW; F4250F7B1B5B6845 CRC64;
MKNEKLPQFQ PHFLAPKYWL FWLGVAIWRS ILCLPYPILR HIGHGFGWLF SHLKVGERRA
AIARRNLELC FPDMPENERE VILQENLRSV GMAIIETGMA WFWSDSRIKK WSKVEGLHYL
KENQKDGIVL VGVHFLTLEL GARIIGLHHP GIGVYRPNDN PLLDWLQTQG RLRSNKDMLD
RKDLRGMIKA LRHEETIWYA PDHDYGRKNA VFVPFFAVPD TCTTTGSYYL LKSSQNSKVI
PFAPLRNKDG SGYTVSISAP VDFTDLQDET AIAARMNQIV EKEIMKDITI YMWLHRRFKT
RPDEKTPSLY D
