ID   KDTA_RICPR              Reviewed;         461 AA.
AC   Q9ZE58;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=3-deoxy-D-manno-octulosonic acid transferase;
DE            Short=Kdo transferase;
DE            EC=2.4.99.12;
DE   AltName: Full=Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase;
GN   Name=waaA; Synonyms=kdtA; OrderedLocusNames=RP089;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
RN   [2]
RP   DOMAIN RPE1.
RX   PubMed=11030655; DOI=10.1126/science.290.5490.347;
RA   Ogata H., Audic S., Barbe V., Artiguenave F., Fournier P.-E., Raoult D.,
RA   Claverie J.-M.;
RT   "Selfish DNA in protein-coding genes of Rickettsia.";
RL   Science 290:347-350(2000).
CC   -!- FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes
CC       the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-
CC       Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate
CC       precursor of lipid A. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) =
CC         alpha-Kdo-(2->6)-lipid IVA + CMP + H(+); Xref=Rhea:RHEA:28066,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58603, ChEBI:CHEBI:60364,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:85987; EC=2.4.99.12;
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 30 subfamily. {ECO:0000305}.
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DR   EMBL; AJ235270; CAA14559.1; -; Genomic_DNA.
DR   PIR; H71717; H71717.
DR   RefSeq; NP_220482.1; NC_000963.1.
DR   RefSeq; WP_004599735.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZE58; -.
DR   SMR; Q9ZE58; -.
DR   STRING; 272947.RP089; -.
DR   CAZy; GT30; Glycosyltransferase Family 30.
DR   EnsemblBacteria; CAA14559; CAA14559; CAA14559.
DR   GeneID; 57569216; -.
DR   KEGG; rpr:RP089; -.
DR   PATRIC; fig|272947.5.peg.89; -.
DR   eggNOG; COG1519; Bacteria.
DR   HOGENOM; CLU_036146_2_0_5; -.
DR   OMA; FIKYEFW; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000002480; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043842; F:Kdo transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.11720; -; 1.
DR   InterPro; IPR007507; Glycos_transf_N.
DR   InterPro; IPR038107; Glycos_transf_N_sf.
DR   InterPro; IPR039901; Kdotransferase.
DR   PANTHER; PTHR42755; PTHR42755; 1.
DR   Pfam; PF04413; Glycos_transf_N; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Lipopolysaccharide biosynthesis;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..461
FT                   /note="3-deoxy-D-manno-octulosonic acid transferase"
FT                   /id="PRO_0000080290"
FT   TRANSMEM        2..22
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          47..88
FT                   /note="RPE1 insert"
FT   ACT_SITE        102
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         306..307
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250"
FT   BINDING         347..349
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250"
FT   BINDING         372..375
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250"
FT   SITE            172
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            247
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   461 AA;  52976 MW;  BE027A7C2D34AC28 CRC64;
     MMLLYYTLSF ILLPVYFIII FIRLLIGKED IRRIQERFAI GKQRQNSALD FIQMSVNKEG
     FTDHKTTSYV DMHRNASLMY KLSLERSYAH SLVWIHAASV GEVMTALTLI HNISKLAPNV
     RFLITSWTNA SAKILSTKLP KIATHQFLPI DNVIFTRKFL RNWQPDLGIF IESELWPCTI
     NEGAKYCKLL LINARISNKS FKAWLKRKRF FQLIIKNFSK IIVQSERDLQ KFNALGISDA
     MNLGNIKFAN EKLLVNQEKL SKLILHLDNR RVLVFASTHP EDEEVILPII NNLKEQFIDC
     YIILIPRHPE RIKSIINNCK LHHLSATAKS QNDLPVLNND LYIVDRFGEM GLFFSVATIS
     FIGGSFKQGG HNILEAAYFS NCIIFGPDMS KNTDIAKGIL QNNAAIQIKN GKDLLNTLTS
     LLNANNALKL KTYRENALKF VENNQKKILD EYLQIIKQFL P