ID   LPXB_GEOSL              Reviewed;         384 AA.
AC   Q74AT9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=GSU2261;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(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; AE017180; AAR35637.1; -; Genomic_DNA.
DR   RefSeq; NP_953310.1; NC_002939.5.
DR   RefSeq; WP_010942901.1; NC_002939.5.
DR   AlphaFoldDB; Q74AT9; -.
DR   SMR; Q74AT9; -.
DR   STRING; 243231.GSU2261; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; AAR35637; AAR35637; GSU2261.
DR   KEGG; gsu:GSU2261; -.
DR   PATRIC; fig|243231.5.peg.2292; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_1_7; -.
DR   InParanoid; Q74AT9; -.
DR   OrthoDB; 9801642at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000577; 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   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   HAMAP; MF_00392; LpxB; 1.
DR   InterPro; IPR003835; Glyco_trans_19.
DR   NCBIfam; TIGR00215; lpxB; 1.
DR   PANTHER; PTHR30372; LIPID-A-DISACCHARIDE SYNTHASE; 1.
DR   PANTHER; PTHR30372:SF7; LIPID-A-DISACCHARIDE SYNTHASE; 1.
DR   Pfam; PF02684; LpxB; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..384
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255184"
SQ   SEQUENCE   384 AA;  41842 MW;  636C4BCEB34FA5F1 CRC64;
     MTENTSHRIM IVAGEASGDL HGAGLVREAL RLDPTLSFFG IGGPRMREAG VETLVDSSEM
     AVVGIVEVLA HIGVISRAFM TLRQVIVSNP PDLLILIDYP DFNMLLARVA RRHGVKVLYY
     ISPQVWAWRT GRVKTIGRLV DRMAVVFPFE VPFYERAGVP VSFVGHPLAD RVRPTMGRDE
     ALASFGLDPG RRVVGLFPGS RRGEIAKLFP VILESAQQLR ERYPDIQFIL PLASSLTDGD
     IAPLLAASGL DVTVTQDRVY DVMQVCDAII TVSGTVTLEI ALMGVPMVII YKVSPLTYQV
     GKRLIRVDHI GICNIVAGER VVPELIQDDA SADRIAAEIG RYLDDPAYAE KTRAGLAMVK
     EKLGTGGCSE RVAGIVLEML GKQV
//