LPXB_BORPE
ID LPXB_BORPE Reviewed; 393 AA.
AC Q7VYB7;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 81.
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}; Synonyms=pgsB;
GN OrderedLocusNames=BP1432;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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=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: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00392}.
CC -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000255|HAMAP-
CC Rule:MF_00392}.
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DR EMBL; BX640415; CAE41722.1; -; Genomic_DNA.
DR RefSeq; NP_880174.1; NC_002929.2.
DR RefSeq; WP_010930356.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VYB7; -.
DR SMR; Q7VYB7; -.
DR STRING; 257313.BP1432; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR GeneID; 45388437; -.
DR KEGG; bpe:BP1432; -.
DR PATRIC; fig|257313.5.peg.1535; -.
DR eggNOG; COG0763; Bacteria.
DR HOGENOM; CLU_036577_3_0_4; -.
DR OMA; PTVWAWR; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000002676; 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;
KW Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..393
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_0000190154"
SQ SEQUENCE 393 AA; 42778 MW; B6C206DCF9DF92C6 CRC64;
MSLRIGMVAG EPSGDLLAGR IIAGLQARAP GVHCAGIGGP QMAARGFEAW HPMHALTVFG
YIDAFKRIPS LLSTYGDVKR RLLAEPPSVF VGIDAPDFNL RLEHQLRQAG TPTVHFVGPS
IWAWRYERIN KIRAAVSHML VLFPFEEALY RKEGIPVTYV GHPLAGVIPM QPDRAAARAR
LGIDADARVL AILPGSRSSE IRLLAPRFLQ AAAELVRRDP RLQCVVPMVN PQRRAEFEAI
ATQHPVPGLR CVTAAEGQGE TPVAWSVMEA SNAVLVASGT ATLETALYKR PMVISYVLSP
WMRRIMAWKS GQQRPYLPWV GLPNVLLRDF AVPELLQDEA TPAALAEATW QALTDEAGAA
RIEARFTALH QDLLRDTPAL AAQAILEVAD GAA