LPXM1_SHIFL
ID LPXM1_SHIFL Reviewed; 323 AA.
AC P59198;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Lipid A biosynthesis myristoyltransferase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01944};
GN Name=lpxM1 {ECO:0000255|HAMAP-Rule:MF_01944};
GN Synonyms=msbB, msbB1 {ECO:0000303|PubMed:11994481,
GN ECO:0000303|PubMed:18359815}; OrderedLocusNames=SF1865, S1931;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=M90T / Serotype 5a;
RX PubMed=11994481; DOI=10.4049/jimmunol.168.10.5240;
RA D'Hauteville H., Khan S., Maskell D.J., Kussak A., Weintraub A.,
RA Mathison J., Ulevitch R.J., Wuscher N., Parsot C., Sansonetti P.J.;
RT "Two msbB genes encoding maximal acylation of lipid A are required for
RT invasive Shigella flexneri to mediate inflammatory rupture and destruction
RT of the intestinal epithelium.";
RL J. Immunol. 168:5240-5251(2002).
RN [4]
RP INDUCTION.
RC STRAIN=YSH6000 / Serotype 2a;
RX PubMed=18359815; DOI=10.1128/jb.00151-08;
RA Goldman S.R., Tu Y., Goldberg M.B.;
RT "Differential regulation by magnesium of the two MsbB paralogs of Shigella
RT flexneri.";
RL J. Bacteriol. 190:3526-3537(2008).
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. Can probably also catalyze the transfer of myristate to
CC Kdo(2)-(palmitoleoyl)-lipid IV(A) to form the cold-adapted Kdo(2)-lipid
CC A. {ECO:0000250|UniProtKB:P24205}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-(Kdo)2-lipid IVA + tetradecanoyl-[ACP] =
CC ((9Z)-hexadecenoyl-tetradecanoyl)-(Kdo)2-lipid A + holo-[ACP];
CC Xref=Rhea:RHEA:28434, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:61520, ChEBI:CHEBI:61522, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78477; Evidence={ECO:0000250|UniProtKB:P24205};
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 -!- INDUCTION: Active under both limited and replete magnesium growth
CC conditions and is independent of the PhoP/PhoQ two-component system.
CC {ECO:0000269|PubMed:18359815}.
CC -!- DISRUPTION PHENOTYPE: A msbB1/msbB2 double mutant is impaired in its
CC capacity to cause TNF-alpha production by human monocytes and to cause
CC rupture and inflammatory destruction of the epithelial barrier in the
CC rabbit ligated intestinal loop model of shigellosis. Mutants have no
CC defect in their ability to enter into host epithelial cells.
CC {ECO:0000269|PubMed:11994481}.
CC -!- SIMILARITY: Belongs to the LpxL/LpxM/LpxP family. LpxM subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01944}.
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DR EMBL; AE005674; AAN43422.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17246.1; -; Genomic_DNA.
DR RefSeq; NP_707715.1; NC_004337.2.
DR RefSeq; WP_000448385.1; NZ_WPGW01000041.1.
DR AlphaFoldDB; P59198; -.
DR SMR; P59198; -.
DR STRING; 198214.SF1865; -.
DR EnsemblBacteria; AAN43422; AAN43422; SF1865.
DR EnsemblBacteria; AAP17246; AAP17246; S1931.
DR GeneID; 1027792; -.
DR GeneID; 58389847; -.
DR KEGG; sfl:SF1865; -.
DR KEGG; sfx:S1931; -.
DR PATRIC; fig|198214.7.peg.2223; -.
DR HOGENOM; CLU_049421_1_0_6; -.
DR OrthoDB; 1106624at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00360; UER00486.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 2: Evidence at transcript level;
KW Acyltransferase; Cell inner membrane; Cell membrane;
KW Lipopolysaccharide biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..323
FT /note="Lipid A biosynthesis myristoyltransferase 1"
FT /id="PRO_0000201779"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01944"
FT MOTIF 139..144
FT /note="HXXXXD motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01944"
SQ SEQUENCE 323 AA; 37410 MW; C9D53D1819B6F7B5 CRC64;
METKKNNSEY IPEFDKSFRH PRYWGAWLGV AAMAGIALTP PKFRDPILAR LGRFAGRLGK
SSRRRALINL SLCFPERSEA EREAIVDEMF ATAPQAMAMM AELAIRGPEK IQPRVGWQGL
EIIEEMRRNN EKVIFLVPHG WAVDIPAMLM ASQGQKMAAM FHNQGNPVFD YVWNTVRRRF
GGRLHARNDG IKPFIQSVRQ GYWGYYLPDQ DHGPEHSEFV DFFATYKATL PAIGRLMKVC
RARVVPLFPI YDGKTHRLTI QVRPPMDDLL EADDHTIERR MNEEVEIFVG PRPEQYTWIL
KLLKTRKPGE IQPYKRKDLY PIK
