ID   LPXB_SHESW              Reviewed;         384 AA.
AC   A1RLL4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
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=Sputw3181_2742;
OS   Shewanella sp. (strain W3-18-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=351745;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W3-18-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. W3-18-1.";
RL   Submitted (DEC-2006) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000503; ABM25559.1; -; Genomic_DNA.
DR   RefSeq; WP_011790015.1; NC_008750.1.
DR   AlphaFoldDB; A1RLL4; -.
DR   SMR; A1RLL4; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   GeneID; 77270153; -.
DR   KEGG; shw:Sputw3181_2742; -.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000002597; 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   CDD; cd01635; Glycosyltransferase_GTB-type; 1.
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; Transferase.
FT   CHAIN           1..384
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000049421"
SQ   SEQUENCE   384 AA;  42409 MW;  B746AF9CC8C68D25 CRC64;
     MSKKSQLVFA MVAGELSGDI LGAGLMAALQ KSHPDARFVG IGGPRMEALG FESLFAMEEL
     AVMGIVEVLS RLPRLLKVRA SLIKDITALK PDCFIGIDAP DFNIGLELKL KARGIKTVHY
     VSPSVWAWRP KRIFKIAKAT HMVLSLLPFE KAFYDKHQVP CTFVGHTLAD DIPLRSDKAA
     ARQLLELDAD AEYLAILPGS RGGELKQLAE PFVKAALLIK ENFPDIRFVT PLVNQKRRDQ
     FEQALKDHAP DLEIHMVEGK SREVMTAADG ILLASGTATL EAMLVKRPMV VAYRVSPLTY
     RIAKSMMQVN RFSLPNLLAG KDVVPELIQD DCTPEKIAAA VTVELNRDFA PLNAEFERLH
     QMLRCDASQK AADAVMRLVE TKEG
//