ID   LPXB_RICBR              Reviewed;         381 AA.
AC   Q1RIC1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=RBE_0812;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(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; CP000087; ABE04893.1; -; Genomic_DNA.
DR   RefSeq; WP_011477480.1; NC_007940.1.
DR   AlphaFoldDB; Q1RIC1; -.
DR   SMR; Q1RIC1; -.
DR   STRING; 336407.RBE_0812; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   PRIDE; Q1RIC1; -.
DR   EnsemblBacteria; ABE04893; ABE04893; RBE_0812.
DR   KEGG; rbe:RBE_0812; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_2_0_5; -.
DR   OMA; PTVWAWR; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001951; 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; Transferase.
FT   CHAIN           1..381
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255217"
SQ   SEQUENCE   381 AA;  43782 MW;  D0638A415D4C40DE CRC64;
     MKKIYFIAGE ASGDFAGGRI IRNLKADKEL KIIGIGGRNM EEAGNFESLF PISEINLMGF
     FEVIPHIFRI KKLINKTVED IIDNKPDILI TIDSPGFTYR VAAKVRERLP ELKMIHIVAP
     SVWAYKEGRA AKYAKIYNCL FALLPFEPPY FTKVGLDCRY IGHPIMEQEF YSDKVALRQE
     LEIDEDTKVL CVTLGSRKGE ILRHLPIFIP AIEKVYDDHK KKLMVIFPLA NPDHERIIKP
     FLEKVRFNYI FSYERLKSYA VSDLALAKSG TNTLEIAASG TPMIVAYKVN IFSFIIIRLL
     IKIKYVTLIN IIGNREIIPE FIQFNCEANL ISDKLKELLL NPQEVDKQIT ESHKILQELG
     FKSNIYPSYL ATKIIRQEFL K