LPXB_HAEI8
ID LPXB_HAEI8 Reviewed; 390 AA.
AC Q4QLM6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 79.
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}; OrderedLocusNames=NTHI1220;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S. Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX88071.1; -; Genomic_DNA.
DR RefSeq; WP_011272365.1; NC_007146.2.
DR AlphaFoldDB; Q4QLM6; -.
DR SMR; Q4QLM6; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR EnsemblBacteria; AAX88071; AAX88071; NTHI1220.
DR KEGG; hit:NTHI1220; -.
DR HOGENOM; CLU_036577_3_0_6; -.
DR OMA; PTVWAWR; -.
DR OrthoDB; 1258510at2; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000002525; 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; Transferase.
FT CHAIN 1..390
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_0000255186"
SQ SEQUENCE 390 AA; 43569 MW; 9DBAEF9AEE82E2A0 CRC64;
MNKTNPTIAL VAGEVSGDIL GAGLIRQLKA HYPNARFIGI AGTRMLAEGC KTLVDMEELS
VMGLAEILKH LPRLLKIRKN VIQTMLQEKP DVYIGIDAPD FNLDVELKLK ANGIKTIHYV
SPSVWAWRQN RIHKIAKATH QVLAFLPFEK AFYDKFNVPC RFIGHTMADA IPLKPNRAEA
CQMLQIDPAQ RYLAILVGSR GSEVEFLAEP FLKTALLLKE QFPDLQFLVP LVNEKRRIQF
EAIKAKIAPN LDLHLIDGNA RQAMIAADAT LLASGTAALE AMLCKSPMVV GYRMKPLTYF
LAKRLVKTDY ISLPNLLANE MLVPEMIQEE CTPELLAEKL SAYLSDDESA VKNRHILIQH
FTDLHQKIQC NADKQAAQAV IDLLEGTENV