LPXB_COXBR
ID LPXB_COXBR Reviewed; 376 AA.
AC A9NCA7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=COXBURSA331_A0735;
OS Coxiella burnetii (strain RSA 331 / Henzerling II).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=360115;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 331 / Henzerling II;
RA Seshadri R., Samuel J.E.;
RT "Genome sequencing of phylogenetically and phenotypically diverse Coxiella
RT burnetii isolates.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000890; ABX78484.1; -; Genomic_DNA.
DR RefSeq; WP_010957694.1; NC_010117.1.
DR AlphaFoldDB; A9NCA7; -.
DR SMR; A9NCA7; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR KEGG; cbs:COXBURSA331_A0735; -.
DR HOGENOM; CLU_036577_3_1_6; -.
DR OMA; PTVWAWR; -.
DR UniPathway; UPA00973; -.
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; Transferase.
FT CHAIN 1..376
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_1000080277"
SQ SEQUENCE 376 AA; 41955 MW; 6D1A160A53A58E7F CRC64;
MSNKSVLLIA GEPSGDLLGA HLAQSLKSLE PNLKLAGMGG KRMREAGVEV FINADKLAVV
GLLEILRQFR DIRHAMQTLK RYFKKTPPDL VVFIDYPGFN LHMAKQAKKA GIKVLYYVSP
QIWAWRYGRI KKIKKYVDHM AVLFDFEEKL YQKENVPVSF VGHPLANAPT PSLSRNEICK
QFNLDPDKPI VALFPGSREQ EINKLLPMMV QAGKLIQTQI PTVQFILPLA LNLALDKIRP
FLSPEIKVIQ NDISYVLAIA HAAVAASGTV TLEIALQQVP LVIIYKVAPL TFWLGKKLIR
LSFIGLCNLV SPEPVAVELL QQDATPQAIA DEVFQLLNNH NYRQSIIGKL GHLRPQLDRG
NAAQNVAKVV HNLIFS