ID   LPXB_PSET1              Reviewed;         385 AA.
AC   Q3IIW8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=PSHAa2017;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA   Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(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; CR954246; CAI87073.1; -; Genomic_DNA.
DR   RefSeq; WP_011328675.1; NC_007481.1.
DR   AlphaFoldDB; Q3IIW8; -.
DR   SMR; Q3IIW8; -.
DR   STRING; 326442.PSHAa2017; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; CAI87073; CAI87073; PSHAa2017.
DR   KEGG; pha:PSHAa2017; -.
DR   PATRIC; fig|326442.8.peg.1944; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_0_6; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   BioCyc; PHAL326442:PSHA_RS09965-MON; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000006843; Chromosome I.
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..385
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255206"
SQ   SEQUENCE   385 AA;  42491 MW;  5EB17FDA1F34F8B2 CRC64;
     MNKDQKQLRI GIVAGELSGD ILGEGLIKAL KKHFPDAIFE GIAGPKMQAQ GCNTLYDMDE
     LSVMGLVEVL GRLPRLLKIR KQLVQHFIDN PPDVFIGIDA PDFNLRVEKP LKDAGIKTVQ
     YVSPSVWAWR EKRIHTISAA TNLVLALLPF EKEFYDKHQV PCTFVGHTLA DDIALEHDDS
     KARKELGLSP DDKVLALLPG SRGSEVGLLS ETYIKTAVQL QAQNPALKIV VPLVNAKRKA
     QFTEILNATA PTLKISLLDG QSKQAMQAAD AILLASGTAT LEGMLYKKPM VVGYKIKPLS
     YWIFKTLFTF NIKYFSLPNL LADEELVPEF LQSECNVANL TQALTPMLNT DNQALKARFL
     AIHKKIRLNA SEQAANAVAE LINAN