ID   D7GK88_ECOLX            Unreviewed;       314 AA.
AC   D7GK88;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   22-FEB-2023, entry version 38.
DE   RecName: Full=Lipid A biosynthesis myristoyltransferase {ECO:0000256|HAMAP-Rule:MF_01944};
DE            EC=2.3.1.243 {ECO:0000256|HAMAP-Rule:MF_01944};
DE   AltName: Full=Kdo(2)-lauroyl-lipid IV(A) myristoyltransferase {ECO:0000256|HAMAP-Rule:MF_01944};
GN   Name=msbB {ECO:0000313|EMBL:CBL93316.1};
GN   Synonyms=lpxM {ECO:0000256|HAMAP-Rule:MF_01944};
GN   ORFNames=ETEC1392/75_p1018_059 {ECO:0000313|EMBL:CBL93316.1};
OS   Escherichia coli ETEC 1392/75.
OG   Plasmid p1081 {ECO:0000313|EMBL:CBL93316.1,
OG   ECO:0000313|Proteomes:UP000464056}.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=762608 {ECO:0000313|EMBL:CBL93316.1, ECO:0000313|Proteomes:UP000464056};
RN   [1] {ECO:0000313|EMBL:CBL93316.1, ECO:0000313|Proteomes:UP000464056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ETEC 1392/75 {ECO:0000313|EMBL:CBL93316.1,
RC   ECO:0000313|Proteomes:UP000464056};
RC   PLASMID=p1081 {ECO:0000313|EMBL:CBL93316.1,
RC   ECO:0000313|Proteomes:UP000464056};
RX   PubMed=20802035; DOI=10.1128/JB.00710-10;
RA   Crossman L.C., Chaudhuri R.R., Beatson S.A., Wells T.J., Desvaux M.,
RA   Cunningham A.F., Petty N.K., Mahon V., Brinkley C., Hobman J.L.,
RA   Savarino S.J., Turner S.M., Pallen M.J., Penn C.W., Parkhill J.,
RA   Turner A.K., Johnson T.J., Thomson N.R., Smith S.G., Henderson I.R.;
RT   "A commensal gone bad: complete genome sequence of the prototypical
RT   enterotoxigenic Escherichia coli strain H10407.";
RL   J. Bacteriol. 192:5822-5831(2010).
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:0000256|HAMAP-Rule:MF_01944}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-(dodecanoyl)-lipid IVA (E.
CC         coli) + tetradecanoyl-[ACP] = alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid
CC         A (E. coli) + holo-[ACP]; Xref=Rhea:RHEA:28438, Rhea:RHEA-COMP:9648,
CC         Rhea:RHEA-COMP:9685, ChEBI:CHEBI:58540, ChEBI:CHEBI:61524,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78477; EC=2.3.1.243;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01944};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01944}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01944}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01944}.
CC   -!- SIMILARITY: Belongs to the LpxL/LpxM/LpxP family. LpxM subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01944}.
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DR   EMBL; FN822745; CBL93316.1; -; Genomic_DNA.
DR   RefSeq; WP_001420717.1; NC_014232.1.
DR   RefSeq; YP_003717572.1; NC_014232.1.
DR   AlphaFoldDB; D7GK88; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00360; UER00486.
DR   Proteomes; UP000464056; Plasmid p1081.
DR   GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; LIPID A BIOSYNTHESIS LAUROYL ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR30606:SF4; LIPID A BIOSYNTHESIS MYRISTOYLTRANSFERASE; 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 {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_01944};
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW   Rule:MF_01944};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01944};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01944};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01944};
KW   Plasmid {ECO:0000313|EMBL:CBL93316.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01944}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_01944};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01944}.
FT   MOTIF           137..142
FT                   /note="HXXXXD motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01944"
SQ   SEQUENCE   314 AA;  36496 MW;  616A1E8DEE64C779 CRC64;
     MKKYKSEFIP EFKKNYLSPV YWSTWFLLGM IAGISMFPPS FRDPVLAKIG RWAGRLSKKA
     RRRATINLSL CFPEKSDTER EIIVDKMFAT ALQSIVMMAE LAIRGPEKFQ KRVFWKGLEI
     LEEIRHNNRN VIFLVPHGWS VDIPAMLLAA QGEKMAAMFH QQRNPVIDYI WNSVRRKFGG
     RLHAREDGIK PFIQSVRQGY WGYYLPDQDH GPEYSEFADF FATYKATLPI IGRLMNISQA
     MIIPLFPVYD EKKHLLTIEI RPPMDACIAS ADNKMIARQM NKTVEILVGP HPEQYVWVLK
     LLKTRKLNEA DPYP
//