LPXM_HAEIN
ID LPXM_HAEIN Reviewed; 318 AA.
AC P44567;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Lipid A biosynthesis myristoyltransferase {ECO:0000255|HAMAP-Rule:MF_01944};
DE EC=2.3.1.243 {ECO:0000255|HAMAP-Rule:MF_01944};
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}; Synonyms=msbB;
GN OrderedLocusNames=HI_0199;
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).
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. {ECO:0000255|HAMAP-Rule:MF_01944}.
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 -!- 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}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01944}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01944}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01944}.
CC -!- SIMILARITY: Belongs to the LpxL/LpxM/LpxP family. LpxM subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01944}.
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DR EMBL; L42023; AAC21868.1; -; Genomic_DNA.
DR PIR; I64053; I64053.
DR RefSeq; NP_438368.1; NC_000907.1.
DR RefSeq; WP_005694093.1; NC_000907.1.
DR AlphaFoldDB; P44567; -.
DR SMR; P44567; -.
DR STRING; 71421.HI_0199; -.
DR EnsemblBacteria; AAC21868; AAC21868; HI_0199.
DR KEGG; hin:HI_0199; -.
DR PATRIC; fig|71421.8.peg.204; -.
DR eggNOG; COG1560; Bacteria.
DR HOGENOM; CLU_049421_1_0_6; -.
DR OMA; GKMHARQ; -.
DR PhylomeDB; P44567; -.
DR BioCyc; HINF71421:G1GJ1-210-MON; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00360; UER00486.
DR Proteomes; UP000000579; 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:0019107; F:myristoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Acyltransferase; Cell inner membrane; Cell membrane;
KW Lipopolysaccharide biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..318
FT /note="Lipid A biosynthesis myristoyltransferase"
FT /id="PRO_0000201778"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01944"
FT MOTIF 145..150
FT /note="HXXXXD motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01944"
SQ SEQUENCE 318 AA; 36883 MW; DE59952D78719445 CRC64;
MSDNQQNLRL TARVGYEAHF SWSYLKPQYW GIWLGIFFLL LLAFVPFRLR DKLTGKLGIW
IGHKAKKQRT RAQTNLQYCF PHWTEQQREQ VIDKMFAVVA QVMFGIGEIA IRSKKHLQKR
SEFIGLEHIE QAKAEGKNII LMVPHGWAID ASGIILHTQG MPMTSMYNPH RNPLVDWLWT
ITRQRFGGKM HARQNGIKPF LSHVRKGEMG YYLPDEDFGA EQSVFVDFFG TYKATLPGLN
KMAKLSKAVV IPMFPRYNAE TGKYEMEIHP AMNLSDDPEQ SARAMNEEIE SFVTPAPEQY
VWILQLLRTR KDGEDLYD
