LPXP_SHIFL
ID LPXP_SHIFL Reviewed; 306 AA.
AC P0ACV3; P76522; P76949;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Lipid A biosynthesis palmitoleoyltransferase {ECO:0000255|HAMAP-Rule:MF_01943};
DE EC=2.3.1.242 {ECO:0000255|HAMAP-Rule:MF_01943};
DE AltName: Full=Kdo(2)-lipid IV(A) palmitoleoyltransferase {ECO:0000255|HAMAP-Rule:MF_01943};
GN Name=lpxP {ECO:0000255|HAMAP-Rule:MF_01943}; Synonyms=ddg;
GN OrderedLocusNames=SF2444, S2582;
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).
CC -!- FUNCTION: Catalyzes the transfer of palmitoleate from palmitoleoyl-acyl
CC carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-
CC (palmitoleoyl)-lipid IV(A). {ECO:0000255|HAMAP-Rule:MF_01943}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-[ACP] + alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-
CC lipid IVA = (9Z)-hexadecenoyl-(Kdo)2-lipid IVA + holo-[ACP];
CC Xref=Rhea:RHEA:44012, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:10800,
CC ChEBI:CHEBI:60365, ChEBI:CHEBI:61520, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:83989; EC=2.3.1.242; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01943};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01943}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01943}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01943}.
CC -!- SIMILARITY: Belongs to the LpxL/LpxM/LpxP family. LpxP subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01943}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN43955.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP17765.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN43955.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP17765.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_708248.3; NC_004337.2.
DR RefSeq; WP_000484404.1; NZ_WPGW01000027.1.
DR AlphaFoldDB; P0ACV3; -.
DR SMR; P0ACV3; -.
DR STRING; 198214.SF2444; -.
DR EnsemblBacteria; AAN43955; AAN43955; SF2444.
DR EnsemblBacteria; AAP17765; AAP17765; S2582.
DR GeneID; 1023448; -.
DR GeneID; 66673752; -.
DR KEGG; sfl:SF2444; -.
DR KEGG; sfx:S2582; -.
DR PATRIC; fig|198214.7.peg.2918; -.
DR HOGENOM; CLU_049421_1_0_6; -.
DR OMA; FWFHRRF; -.
DR OrthoDB; 1106624at2; -.
DR UniPathway; UPA00030; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008951; F:palmitoleoyl [acyl-carrier-protein]-dependent acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:InterPro.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009409; P:response to cold; IEA:InterPro.
DR CDD; cd07984; LPLAT_LABLAT-like; 1.
DR HAMAP; MF_01942; Lipid_A_LpxL_LpxP; 1.
DR HAMAP; MF_01943; Lipid_A_LpxP; 1.
DR InterPro; IPR004960; LipA_acyltrans.
DR InterPro; IPR011920; Lipid_A_LpxL_LpxP.
DR InterPro; IPR030857; Lipid_A_LpxP.
DR PANTHER; PTHR30606; PTHR30606; 1.
DR Pfam; PF03279; Lip_A_acyltrans; 1.
DR PIRSF; PIRSF026649; MsbB; 1.
DR TIGRFAMs; TIGR02207; lipid_A_htrB; 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..306
FT /note="Lipid A biosynthesis palmitoleoyltransferase"
FT /id="PRO_0000201782"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01943"
FT MOTIF 132..137
FT /note="HXXXXD motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01943"
SQ SEQUENCE 306 AA; 35493 MW; 58327F3D96C9E7B6 CRC64;
MFPQCKFSRE FLHPRYWLTW FGLGVLWLWV QLPYPVLCFL GTRIGAMARP FLKRRESIAR
KNLELCFPQH SAEEREKMIA ENFRSLGMAL VETGMAWFWP DSRVRKWFDV EGLDNLKRAQ
MQNRGVMVVG VHFMSLELGG RVMGLCQPMM ATYRPHNNQL MEWVQTRGRM RSNKAMIGRN
NLRGIVGALK KGEAVWFAPD QDYGRKGSSF APFFAVENVA TTNGTYVLSR LSGAAMLTVT
MVRKADYSGY RLFITPEMEG YPTDENQAAA YMNKIIEKEI MRAPEQYLWI HRRFKTRPVG
ESSLYI
