ID   LPXB_RICB8              Reviewed;         381 AA.
AC   A8GU85;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=A1I_05190;
OS   Rickettsia bellii (strain OSU 85-389).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=391896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OSU 85-389;
RA   Madan A., Lee H., Madan A., Yoon J.-G., Ryu G.-Y., Dasch G., Ereemeva M.;
RT   "Complete genome sequencing of Rickettsia bellii.";
RL   Submitted (SEP-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; CP000849; ABV79367.1; -; Genomic_DNA.
DR   RefSeq; WP_011477480.1; NC_009883.1.
DR   AlphaFoldDB; A8GU85; -.
DR   SMR; A8GU85; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   KEGG; rbo:A1I_05190; -.
DR   HOGENOM; CLU_036577_2_0_5; -.
DR   UniPathway; UPA00973; -.
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   NCBIfam; TIGR00215; lpxB; 1.
DR   PANTHER; PTHR30372; LIPID-A-DISACCHARIDE SYNTHASE; 1.
DR   PANTHER; PTHR30372:SF4; LIPID-A-DISACCHARIDE SYNTHASE, MITOCHONDRIAL-RELATED; 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..381
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000049412"
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
//