(data stored in SCRATCH zone)

SWISSPROT: C8U1Q0_ECO10

ID   C8U1Q0_ECO10            Unreviewed;       382 AA.
AC   C8U1Q0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 60.
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   ECO:0000313|EMBL:BAI29058.1};
GN   OrderedLocusNames=ECO103_0180 {ECO:0000313|EMBL:BAI29058.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29058.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29058.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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; AP010958; BAI29058.1; -; Genomic_DNA.
DR   RefSeq; WP_000139659.1; NC_013353.1.
DR   SMR; C8U1Q0; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; BAI29058; BAI29058; ECO103_0180.
DR   KEGG; eoh:ECO103_0180; -.
DR   HOGENOM; HOG000018003; -.
DR   KO; K00748; -.
DR   OMA; PTVWAWR; -.
DR   BioCyc; ECOL585395:ECO103_RS00920-MONOMER; -.
DR   UniPathway; UPA00359; UER00481.
DR   Proteomes; UP000000959; 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; C8U1Q0.
DR   SWISS-2DPAGE; C8U1Q0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00392,
KW   ECO:0000256|SAAS:SAAS00702242};
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}.
SQ   SEQUENCE   382 AA;  42416 MW;  6FD4212BCCE6C57E CRC64;
     MTEQRPLTIA LVAGETSGDI LGAGLIRALK ERVPNARFVG VAGPRMQAEG CEAWYEMEEL
     AVMGIVEVLG RLRRLLHIRA DLTKRFGELK PDIFVGIDAP DFNITLEGNL KKQGIKTIHY
     VSPSVWAWRQ KRVFKIGRAT DLVLAFLPFE KAFYDKYNVP CRFIGHTMAD AMPLDPDKNA
     ARDVLGIPHD AHCLALLPGS RGAEVEMLSA DFLKTAQLLR QTYPDLEIVV PLVNAKRREQ
     FERIKAEVAP DLSVHLLDGM GREAMVASDA ALLASGTAAL ECMLAKCPMV VGYRMKPFTF
     WLAKRLVKTD YVSLPNLLAG RELVKELLQE ECEPQKLAAA LLPLLANGKT SHAMHDTFRE
     LHQQIRCNAD EQAAQAVLEL AQ
//

If you have problems or comments...

PBIL Back to PBIL home page