ID   LPXB_NITOC              Reviewed;         387 AA.
AC   Q3JAC1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=Noc_1753;
OS   Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS   11848 / C-107).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Nitrosococcus.
OX   NCBI_TaxID=323261;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107;
RX   PubMed=16957257; DOI=10.1128/aem.00463-06;
RA   Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA   Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA   Vergez L.M., Ward B.B.;
RT   "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT   oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL   Appl. Environ. Microbiol. 72:6299-6315(2006).
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; CP000127; ABA58225.1; -; Genomic_DNA.
DR   RefSeq; WP_002808842.1; NC_007484.1.
DR   AlphaFoldDB; Q3JAC1; -.
DR   SMR; Q3JAC1; -.
DR   STRING; 323261.Noc_1753; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; ABA58225; ABA58225; Noc_1753.
DR   KEGG; noc:Noc_1753; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_1_6; -.
DR   OMA; PTVWAWR; -.
DR   OrthoDB; 1258510at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000006838; 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..387
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255203"
SQ   SEQUENCE   387 AA;  43005 MW;  67CD25C95187726C CRC64;
     MENSAPLVAI VAGEASGDQH AAHLIREVKK IAPGVRFGGI AGPQMRAAGV EPLFDSSRLA
     VVGLVEVLSH LNEIYGAMQK MRHFLEEKHP DLLILVDYPE FNLRLAKRAK TLGIKVLYYI
     SPQVWAWRQY RVHQIGQVVD MMAVVLPFEV PFYEQAGVPV NFVGHPLQHE VKSKFNRNEA
     VVEFGFNPCC KTLGLLPGSR HSEIKRLLPV LLEAAERIYS EEPEIQYLLP LAATLKEIDL
     APYLKGYRLP LRVIPDRSYD VMAACDAMVA ASGTVTLEAA LMGVPLVVIY KMNSLSYWMG
     RLLIKVDHIA LCNIIAGEGV APELIQQDAS PERIALEALN LLRDKERRQT MQQKFYAIKH
     KLGAGAQRTI AELTVAMLEG ENLGRAS