LPXM2_SHIFL
ID LPXM2_SHIFL Reviewed; 314 AA.
AC O06659; Q9AFL5; Q9AJU9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Lipid A biosynthesis myristoyltransferase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01944};
GN Name=lpxM2 {ECO:0000255|HAMAP-Rule:MF_01944};
GN Synonyms=msbB, msbB2 {ECO:0000303|PubMed:11994481,
GN ECO:0000303|PubMed:18359815}; OrderedLocusNames=CP0238;
OS Shigella flexneri.
OG Plasmid pWR100, Plasmid pMYSH6000, and Plasmid pCP301.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11115111; DOI=10.1046/j.1365-2958.2000.02179.x;
RA Buchrieser C., Glaser P., Rusniok C., Nedjari H., d'Hauteville H.,
RA Kunst F., Sansonetti P.J., Parsot C.;
RT "The virulence plasmid pWR100 and the repertoire of proteins secreted by
RT the type III secretion apparatus of Shigella flexneri.";
RL Mol. Microbiol. 38:760-771(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11292750; DOI=10.1128/iai.69.5.3271-3285.2001;
RA Venkatesan M.M., Goldberg M.B., Rose D.J., Grotbeck E.J., Burland V.,
RA Blattner F.R.;
RT "Complete DNA sequence and analysis of the large virulence plasmid of
RT Shigella flexneri.";
RL Infect. Immun. 69:3271-3285(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a; PLASMID=pCP301;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 84-314.
RC STRAIN=YSH6000 / Serotype 2a; PLASMID=pMYSH6000;
RX PubMed=9171415; DOI=10.1128/jb.179.11.3670-3675.1997;
RA Radnedge L., Davis M.A., Youngren B., Austin S.J.;
RT "Plasmid maintenance functions of the large virulence plasmid of Shigella
RT flexneri.";
RL J. Bacteriol. 179:3670-3675(1997).
RN [5]
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 [6]
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: Induced under limited magnesium growth conditions by the
CC PhoP/PhoQ two-component system. {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 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC05860.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL391753; CAC05860.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF348706; AAK18563.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72336.1; -; Genomic_DNA.
DR EMBL; U82621; AAB58154.1; -; Genomic_DNA.
DR RefSeq; NP_085407.1; NC_002698.1.
DR RefSeq; NP_858371.1; NC_004851.1.
DR RefSeq; WP_004996485.1; NZ_WPGW01000147.1.
DR RefSeq; YP_006960300.1; NC_019197.1.
DR RefSeq; YP_009062542.1; NC_024996.1.
DR AlphaFoldDB; O06659; -.
DR SMR; O06659; -.
DR STRING; 198214.CP0238; -.
DR EnsemblBacteria; AAL72336; AAL72336; SF_p0238.
DR GeneID; 1238039; -.
DR GeneID; 58462862; -.
DR KEGG; sfl:CP0238; -.
DR PATRIC; fig|198214.7.peg.5500; -.
DR HOGENOM; CLU_049421_1_0_6; -.
DR OMA; GKMHARQ; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00360; UER00486.
DR PRO; PR:O06659; -.
DR Proteomes; UP000001006; Plasmid pCP301.
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; Plasmid; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..314
FT /note="Lipid A biosynthesis myristoyltransferase 2"
FT /id="PRO_0000201780"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01944"
FT MOTIF 137..142
FT /note="HXXXXD motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01944"
SQ SEQUENCE 314 AA; 36584 MW; 15F8C6CA972857BA CRC64;
MKKYKSEFIP EFKKNYLSPV YWFTWFVLGM IAGISMFPPS FRDPVLAKIG RWVGRLSRKA
RRRATINLSL CFPEKSDTER EIIVDNMFAT ALQSIVMMAE LAIRGPEKFQ KRVFWKGLEI
LEEIRHNNRN VIFLVPHGWS VDIPAMLLAA QGEKMAAMFH QQRNPVIDYV WNSVRRKFGG
RLHSREDGIK PFIQSVRQGY WGYYLPDQDH GPEYSEFADF FATYKATLPI IGRLMNISQA
MIIPLFPVYD EKKHFLTIEV RPPMDACIAS ADNKMIARQM NKTVEILVGS HPEQYIWVLK
LLKTRKSNEA DPYP
