ID   KDTA_RICFE              Reviewed;         464 AA.
AC   Q4UND5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=RF_0072;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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       {ECO:0000305}.
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DR   EMBL; CP000053; AAY60923.1; -; Genomic_DNA.
DR   RefSeq; WP_011270427.1; NC_007109.1.
DR   AlphaFoldDB; Q4UND5; -.
DR   SMR; Q4UND5; -.
DR   STRING; 315456.RF_0072; -.
DR   CAZy; GT30; Glycosyltransferase Family 30.
DR   EnsemblBacteria; AAY60923; AAY60923; RF_0072.
DR   KEGG; rfe:RF_0072; -.
DR   eggNOG; COG1519; Bacteria.
DR   HOGENOM; CLU_036146_2_0_5; -.
DR   OMA; FIKYEFW; -.
DR   OrthoDB; 1163086at2; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000008548; 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   InterPro; IPR005728; Rickett_RPE.
DR   PANTHER; PTHR42755; PTHR42755; 1.
DR   Pfam; PF04413; Glycos_transf_N; 1.
DR   TIGRFAMs; TIGR01045; RPE1; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Lipopolysaccharide biosynthesis;
KW   Membrane; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..464
FT                   /note="3-deoxy-D-manno-octulosonic acid transferase"
FT                   /id="PRO_0000286456"
FT   TRANSMEM        2..22
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          47..93
FT                   /note="RPE1 insert"
FT   ACT_SITE        107
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         311..312
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250"
FT   BINDING         352..354
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250"
FT   BINDING         377..380
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250"
FT   SITE            177
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            252
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   464 AA;  52959 MW;  A8737E3670F53F3E CRC64;
     MMLLYYALSF ILLPIYFIII LIRLLIGKED IRRIQERFAI GKHRQVYSLD FLHNEANKER
     FKGDTERRTA AYTSVREDSS TGSTSKLPLE ASYARSLIWI HAASVGESMA ALTLISNISK
     RYPDIRFLVT SWTNSSAKIL TAKLPKIAVH QFLPIDNIIF TRKFLKNWQP NLGIFIESEL
     WPCTINEGAR QCKLLLVNAR ISDKSFKAWL KRKSFFQLIL KNFSKIIVQS ERDLQKFNEL
     GISDAINLGN IKFANEKLPV NQEELSKLSS HLDNRQVVVF ASTHPEDEEV ILPIIKNLKE
     QFLDCYIILI PRHPERVKSI IDNCKSHNLS ATAKSQNDLP VLSDDIYIVD RFGEMGLFFS
     VATISFIGGS FKQGGHNILE AAYFSNCIIF GPDMSKNTDI AKGVLQNEAA IQIKNGEDLL
     TKLTYLLSPN NSLELKAYRE NALKFVENNQ KVLDEYLQVI TKFL