ID   D7GK88_ECOLX            Unreviewed;       314 AA.
AC   D7GK88;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAY-2015, entry version 14.
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}.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=762608 {ECO:0000313|EMBL:CBL93316.1};
RN   [1] {ECO:0000313|EMBL:CBL93316.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ETEC 1392/75 {ECO:0000313|EMBL:CBL93316.1};
RC   PLASMID=p1081 {ECO:0000313|EMBL:CBL93316.1};
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).
RN   [2] {ECO:0000313|EMBL:CBL93316.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ETEC 1392/75 {ECO:0000313|EMBL:CBL93316.1};
RC   PLASMID=p1081 {ECO:0000313|EMBL:CBL93316.1};
RA   Aslett M.A.;
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of myristate from myristoyl-acyl
CC       carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form
CC       Kdo(2)-lipid A. {ECO:0000256|HAMAP-Rule:MF_01944}.
CC   -!- CATALYTIC ACTIVITY: A tetradecanoyl-[acyl-carrier protein] +
CC       (Kdo)(2)-(dodecanoyl)-lipid IV(A) = Kdo(2)-lipid A + a holo-[acyl-
CC       carrier protein]. {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;
CC       KDO(2)-lipid A from CMP-3-deoxy-D-manno-octulosonate and lipid
CC       IV(A): step 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   GeneID; 9292782; -.
DR   KEGG; pg:9292782; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00360; UER00486.
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-HAMAP.
DR   GO; GO:0019107; F:myristoyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_01944; Lipid_A_LpxM; 1.
DR   InterPro; IPR004960; LipA_acyltrans.
DR   InterPro; IPR011921; Lipid_A_MsbB.
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|HAMAP-Rule:MF_01944,
KW   ECO:0000313|EMBL:CBL93316.1};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01944};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01944};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01944};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01944};
KW   Plasmid {ECO:0000313|EMBL:CBL93316.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01944,
KW   ECO:0000313|EMBL:CBL93316.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01944};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01944}.
FT   TRANSMEM     17     37       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01944}.
FT   MOTIF       137    142       HXXXXD motif. {ECO:0000256|HAMAP-Rule:
FT                                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
//