(data stored in SCRATCH zone)

SWISSPROT: A0A0E1NX07_YERPA

ID   A0A0E1NX07_YERPA        Unreviewed;       394 AA.
AC   A0A0E1NX07;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   16-JAN-2019, entry version 27.
DE   RecName: Full=Lipid-A-disaccharide synthase {ECO:0000256|HAMAP-Rule:MF_00392, ECO:0000256|SAAS:SAAS00702238};
DE            EC=2.4.1.182 {ECO:0000256|HAMAP-Rule:MF_00392, ECO:0000256|SAAS:SAAS00702238};
GN   Name=lpxB {ECO:0000256|HAMAP-Rule:MF_00392};
GN   OrderedLocusNames=YPA_0533 {ECO:0000313|EMBL:ABG12501.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12501.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12501.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12501.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Condensation of UDP-2,3-diacylglucosamine and 2,3-
CC       diacylglucosamine-1-phosphate to form lipid A disaccharide, a
CC       precursor of lipid A, a phosphorylated glycolipid that anchors the
CC       lipopolysaccharide to the outer membrane of the cell.
CC       {ECO:0000256|HAMAP-Rule:MF_00392, ECO:0000256|SAAS:SAAS00702254}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-N,3-O-bis(3-hydroxytetradecanoyl)-alpha-D-glucosaminyl
CC         1-phosphate + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-
CC         alpha-D-glucosamine = H(+) + lipid A disaccharide (E. coli) +
CC         UDP; Xref=Rhea:RHEA:22668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57957,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58466, ChEBI:CHEBI:78847;
CC         EC=2.4.1.182; Evidence={ECO:0000256|HAMAP-Rule:MF_00392,
CC         ECO:0000256|SAAS:SAAS01124936};
CC   -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid
CC       IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and
CC       UDP-N-acetyl-alpha-D-glucosamine: step 5/6. {ECO:0000256|HAMAP-
CC       Rule:MF_00392, ECO:0000256|SAAS:SAAS00702246}.
CC   -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00392, ECO:0000256|SAAS:SAAS00702241}.
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; CP000308; ABG12501.1; -; Genomic_DNA.
DR   RefSeq; WP_002212144.1; NZ_CP009906.1.
DR   SMR; A0A0E1NX07; -.
DR   EnsemblBacteria; ABG12501; ABG12501; YPA_0533.
DR   EnsemblBacteria; AJJ81426; AJJ81426; CH58_3385.
DR   KEGG; ypa:YPA_0533; -.
DR   PATRIC; fig|360102.15.peg.3554; -.
DR   KO; K00748; -.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00359; UER00481.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; A0A0E1NX07.
DR   SWISS-2DPAGE; A0A0E1NX07.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00392,
KW   ECO:0000256|SAAS:SAAS00702242, ECO:0000313|EMBL:ABG12501.1};
KW   Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00392,
KW   ECO:0000256|SAAS:SAAS00702231};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00392,
KW   ECO:0000256|SAAS:SAAS00702255};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00392,
KW   ECO:0000256|SAAS:SAAS00702243};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00392,
KW   ECO:0000256|SAAS:SAAS00702258, ECO:0000313|EMBL:ABG12501.1}.
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
//

If you have problems or comments...

PBIL Back to PBIL home page