LPXA_YERPE
ID LPXA_YERPE Reviewed; 262 AA.
AC Q8ZH56; Q0WHY9;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387};
DE Short=UDP-N-acetylglucosamine acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387};
DE EC=2.3.1.129 {ECO:0000255|HAMAP-Rule:MF_00387};
GN Name=lpxA {ECO:0000255|HAMAP-Rule:MF_00387};
GN OrderedLocusNames=YPO1056, y3123, YP_2794;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated
CC glycolipid that anchors the lipopolysaccharide to the outer membrane of
CC the cell. {ECO:0000255|HAMAP-Rule:MF_00387}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine =
CC a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-
CC [ACP]; Xref=Rhea:RHEA:67812, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:57705, ChEBI:CHEBI:64479, ChEBI:CHEBI:78827,
CC ChEBI:CHEBI:173225; EC=2.3.1.129; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00387};
CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC acetyl-alpha-D-glucosamine: step 1/6. {ECO:0000255|HAMAP-
CC Rule:MF_00387}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00387}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00387}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00387}.
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DR EMBL; AL590842; CAL19721.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM86673.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62978.1; -; Genomic_DNA.
DR PIR; AG0129; AG0129.
DR RefSeq; WP_002212143.1; NZ_WHLN01000054.1.
DR RefSeq; YP_002346099.1; NC_003143.1.
DR AlphaFoldDB; Q8ZH56; -.
DR SMR; Q8ZH56; -.
DR STRING; 214092.YPO1056; -.
DR PaxDb; Q8ZH56; -.
DR DNASU; 1148070; -.
DR EnsemblBacteria; AAM86673; AAM86673; y3123.
DR EnsemblBacteria; AAS62978; AAS62978; YP_2794.
DR GeneID; 66844580; -.
DR KEGG; ype:YPO1056; -.
DR KEGG; ypk:y3123; -.
DR KEGG; ypm:YP_2794; -.
DR PATRIC; fig|214092.21.peg.1344; -.
DR eggNOG; COG1043; Bacteria.
DR HOGENOM; CLU_061249_0_0_6; -.
DR OMA; ECVTINR; -.
DR UniPathway; UPA00359; UER00477.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008780; F:acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03351; LbH_UDP-GlcNAc_AT; 1.
DR Gene3D; 1.20.1180.10; -; 1.
DR HAMAP; MF_00387; LpxA; 1.
DR InterPro; IPR029098; Acetyltransf_C.
DR InterPro; IPR037157; Acetyltransf_C_sf.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR010137; Lipid_A_LpxA.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43480; PTHR43480; 1.
DR Pfam; PF13720; Acetyltransf_11; 1.
DR Pfam; PF00132; Hexapep; 2.
DR PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR01852; lipid_A_lpxA; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Reference proteome; Repeat; Transferase.
FT CHAIN 1..262
FT /note="Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine
FT O-acyltransferase"
FT /id="PRO_0000188081"
SQ SEQUENCE 262 AA; 28117 MW; C749FF7F53216DF8 CRC64;
MIDKTAFIHP SSIVEEGAII GAGVYIGPFC IVGSQVEIGA GTELKSHVVV NGITKIGCDN
QIYQFASIGE ANQDLKYAGE PTRVEVGDRN RIRESVTIHR GTTQGGGVTK VGCDNLLMVN
THVAHDCVIG NRCILANNAA LGGHVEIDDY AIIGGMTAIH QFCVIGAHVM VGGCSGITQD
VPPFVIAQGN HATPFGINIE GLKRRGFDKE SLHAIRSAYK LLYRSGRTLD EVKPEIAELA
EQYPVVKAFN DFFARSTRGI IR
