ID   LPXB_SHEPA              Reviewed;         383 AA.
AC   A8H6K3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=Spea_2872;
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-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; CP000851; ABV88190.1; -; Genomic_DNA.
DR   RefSeq; WP_012156095.1; NC_009901.1.
DR   AlphaFoldDB; A8H6K3; -.
DR   SMR; A8H6K3; -.
DR   STRING; 398579.Spea_2872; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; ABV88190; ABV88190; Spea_2872.
DR   KEGG; spl:Spea_2872; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000002608; 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..383
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000080285"
SQ   SEQUENCE   383 AA;  42615 MW;  9FB4E8D3CC1C0FAC CRC64;
     MSSNNPRVFA MVAGEISGDI LGAGLIKALQ KQYPDAKFVG IGGPRMEALG FESIFSYEEL
     AVMGIVEVLS RLPRLLKVRA TLIDELVKTQ PDCFIGIDAP DFNIGLELKL KNRGIKTVHY
     VSPSVWAWRP KRIFKIAKAT DMVLSLLPFE KAFYDEYQVP CTFVGHTLAD DIELESDKAQ
     ARELLGLDKE AEYLAILPGS RGGELKMLAE PFVKAASLIK LRYPDIKFVT PLVNQKRRDQ
     FEQALREHAP DLEIHLIEGH SREVMAAADC ILLASGTATL EAMLVKRPMV VAYRVSPITY
     RIAKGMMLTK RYSLPNLLAD DDVVEELIQA DCTPEKIAAA VATQLDNDFT PMYDRFMQMH
     KGLRCDASAR AADAVIKLVE DNV