LPXB_HAEIN
ID LPXB_HAEIN Reviewed; 390 AA.
AC P45011; P94807;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Lipid-A-disaccharide synthase;
DE EC=2.4.1.182;
GN Name=lpxB; OrderedLocusNames=HI_1060;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP SEQUENCE REVISION.
RA White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RM 7004 / Serotype B;
RX PubMed=8917090; DOI=10.1016/0378-1119(96)00139-4;
RA Servos S., Khan S., Maskell D.;
RT "Cloning and expression of genes encoding lipid A biosynthesis from
RT Haemophilus influenzae type b.";
RL Gene 175:137-141(1996).
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 -!- 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;
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000305}.
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DR EMBL; L42023; AAC22715.1; -; Genomic_DNA.
DR EMBL; X87416; CAA60866.1; -; Genomic_DNA.
DR RefSeq; NP_439218.1; NC_000907.1.
DR RefSeq; WP_010869121.1; NC_000907.1.
DR AlphaFoldDB; P45011; -.
DR SMR; P45011; -.
DR STRING; 71421.HI_1060; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR EnsemblBacteria; AAC22715; AAC22715; HI_1060.
DR KEGG; hin:HI_1060; -.
DR PATRIC; fig|71421.8.peg.1104; -.
DR eggNOG; COG0763; Bacteria.
DR HOGENOM; CLU_036577_3_0_6; -.
DR OMA; PTVWAWR; -.
DR PhylomeDB; P45011; -.
DR BioCyc; HINF71421:G1GJ1-1097-MON; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
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..390
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_0000190168"
FT CONFLICT 342
FT /note="V -> A (in Ref. 3; CAA60866)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="A -> S (in Ref. 3; CAA60866)"
FT /evidence="ECO:0000305"
FT CONFLICT 387..388
FT /note="KE -> TK (in Ref. 3; CAA60866)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 43637 MW; 690BEC98ECFEECCD CRC64;
MNKTNPTIAL VAGEVSGDIL GAGLIRQLKA HYPNARFIGI AGPRMLAEGC ETLVDMEELS
VMGLAEILKH LPRLLKIRKN VIQTMLQEKP DVYIGIDAPD FNLDVELKLK ANGIKTIHYV
SPSVWAWRQN RIHKIAKATH QVLAFLPFEK AFYDKFNVPC RFIGHTMADA IPLKPNRAEA
CQTLQIDPAQ RYLAILVGSR GSEVEFLAEP FLKTALLLKE QFPDLQFLVP LVNEKRRIQF
ETIKAKITPN LDLHLIDGNA RQAMIAADAT LLASGTAALE AMLCKSPMVV GYRMKPLTYF
LAKRLVKTDY ISLPNLLANE MLVPEMIQEE CTPELLAEKL SVYLSDDESA VKNRHVLIQH
FTDLHQKIQC NADKQAAQAV IDLLEGKENV