ID   LPXB_RICAH              Reviewed;         391 AA.
AC   A8GN02;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   02-SEP-2026, entry version 81.
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=A1C_02380;
OS   Rickettsia akari (strain Hartford).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia;
OC   spotted fever group.
OX   NCBI_TaxID=293614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hartford;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia akari.";
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 + UDP + H(+);
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; CP000847; ABV74777.1; -; Genomic_DNA.
DR   RefSeq; WP_012149411.1; NC_009881.1.
DR   AlphaFoldDB; A8GN02; -.
DR   SMR; A8GN02; -.
DR   STRING; 293614.A1C_02380; -.
DR   PaxDb; 293614-A1C_02380; -.
DR   KEGG; rak:A1C_02380; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_2_0_5; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000006830; Chromosome.
DR   GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005543; F:phospholipid binding; IEA:TreeGrafter.
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; Reference proteome; Transferase.
FT   CHAIN           1..391
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000049411"
SQ   SEQUENCE   391 AA;  44141 MW;  F0F4F9007ECECBC1 CRC64;
     MTKVYFIAGE TSGDFIGGRI IQNLKSNKGV EFTGIGGKCM EEAGNFKSLF PITCINLMGF
     VEILPHIFNL KKLIDKTVQD IINSQADLLI TIDSPGFTYR VAKQLRKLLP KLKMIHIVAP
     SVWAYKDGRA VKYAKIYDCL FALLPFEPPY FTKVGLDCRY IGHPIMEQEF YSDKIALREE
     FKIDKNERVL CVTLGSRQGE IRKHLPVFIS SIEEIFKSCN NLKVIFTLAN PAHEAIIKPF
     LEDVQFHYLF SSARLKAYAV ADAALAKSGT NTLEIVASGT PMVVAYQVNL ISFFIIRLLI
     KIKYVTLINI IAGSEIIPEF IQFNCRASLI SNTLQELLFN SKKAYKQVIE SQKILQTLGL
     KSNRSPSYIA AEIIKQEFLE SKIKLLKENS T
//