LPXB_YERPE
ID LPXB_YERPE Reviewed; 394 AA.
AC Q8ZH55; Q0WHY8;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Lipid-A-disaccharide synthase {ECO:0000255|HAMAP-Rule:MF_00392};
DE EC=2.4.1.182 {ECO:0000255|HAMAP-Rule:MF_00392};
GN Name=lpxB {ECO:0000255|HAMAP-Rule:MF_00392};
GN OrderedLocusNames=YPO1057, y3122, YP_2793;
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: Condensation of UDP-2,3-diacylglucosamine and 2,3-
CC diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor
CC of lipid A, a phosphorylated glycolipid that anchors the
CC lipopolysaccharide to the outer membrane of the cell.
CC {ECO:0000255|HAMAP-Rule:MF_00392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl
CC 1-phosphate + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-
CC glucosamine = H(+) + lipid A disaccharide (E. coli) + UDP;
CC Xref=Rhea:RHEA:22668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57957,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58466, ChEBI:CHEBI:78847;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00392};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-
CC glucosamine = a lipid A disaccharide + H(+) + UDP;
CC Xref=Rhea:RHEA:67828, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:137748, ChEBI:CHEBI:176338, ChEBI:CHEBI:176343;
CC EC=2.4.1.182; Evidence={ECO:0000255|HAMAP-Rule:MF_00392};
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 5/6. {ECO:0000255|HAMAP-
CC Rule:MF_00392}.
CC -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000255|HAMAP-
CC Rule:MF_00392}.
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DR EMBL; AL590842; CAL19722.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM86672.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62977.1; -; Genomic_DNA.
DR PIR; AH0129; AH0129.
DR RefSeq; WP_002212144.1; NZ_WUCM01000044.1.
DR RefSeq; YP_002346100.1; NC_003143.1.
DR AlphaFoldDB; Q8ZH55; -.
DR SMR; Q8ZH55; -.
DR STRING; 214092.YPO1057; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR PaxDb; Q8ZH55; -.
DR DNASU; 1148069; -.
DR EnsemblBacteria; AAM86672; AAM86672; y3122.
DR EnsemblBacteria; AAS62977; AAS62977; YP_2793.
DR GeneID; 66844581; -.
DR KEGG; ype:YPO1057; -.
DR KEGG; ypk:y3122; -.
DR KEGG; ypm:YP_2793; -.
DR PATRIC; fig|214092.21.peg.1345; -.
DR eggNOG; COG0763; Bacteria.
DR HOGENOM; CLU_036577_3_0_6; -.
DR OMA; PTVWAWR; -.
DR UniPathway; UPA00359; UER00481.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
DR HAMAP; MF_00392; LpxB; 1.
DR InterPro; IPR003835; Glyco_trans_19.
DR PANTHER; PTHR30372; PTHR30372; 1.
DR Pfam; PF02684; LpxB; 1.
DR TIGRFAMs; TIGR00215; lpxB; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..394
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_0000190197"
SQ SEQUENCE 394 AA; 43261 MW; F4A481D7C188B25C CRC64;
MQNSPLTADC SLNAGRPLTI GLVAGETSGD ILGAGLIRAL KVQVPNARFV GVAGPLMQAE
GCEAWYEMEE LAVMGVVEVL ERLPRLLKIR KDLTQRFSEL SPDVFVGIDA PDFNITLEGR
LKQRGIRTIH YVSPSVWAWR QKRVFKIGKA TDMVLAFLPF EKAFYDRFNV PCRFIGHTMA
DAMPLVPDQQ AARAELGIAP NATCLALLPG SRHSEVEMLS ADFLRTAVIL RDKLPNLEVV
VPLVNSKRRE QFERIKAEIA PDLSVHLLDG KARVAMIASD AALLASGTAA LECMLAKCPM
VVGYRMKPFT FWLAERLVKT PYVSLPNLLA GEELVTELLQ QECQPQKLAG ALLPLLQGGS
EIAALKERFL VLHQSIRCGA DEQAAQAVLE LADR
