ID   KDTA_RICCN              Reviewed;         464 AA.
AC   Q92JE9;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 107.
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=RC0118;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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 (E. coli) + CMP + H(+);
CC         Xref=Rhea:RHEA:28066, ChEBI:CHEBI:15378, ChEBI:CHEBI:58603,
CC         ChEBI:CHEBI:60364, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987;
CC         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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE006914; AAL02656.1; -; Genomic_DNA.
DR   PIR; F97714; F97714.
DR   RefSeq; WP_010976798.1; NC_003103.1.
DR   AlphaFoldDB; Q92JE9; -.
DR   SMR; Q92JE9; -.
DR   CAZy; GT30; Glycosyltransferase Family 30.
DR   GeneID; 928074; -.
DR   KEGG; rco:RC0118; -.
DR   PATRIC; fig|272944.4.peg.140; -.
DR   HOGENOM; CLU_036146_2_0_5; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000000816; Chromosome.
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; 3-Deoxy-D-manno-octulosonic-acid transferase, N-terminal domain; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   InterPro; IPR007507; Glycos_transf_N.
DR   InterPro; IPR038107; Glycos_transf_N_sf.
DR   InterPro; IPR039901; Kdotransferase.
DR   InterPro; IPR005728; RPE1.
DR   NCBIfam; TIGR01045; RPE1; 1.
DR   PANTHER; PTHR42755:SF1; 3-DEOXY-D-MANNO-OCTULOSONIC ACID TRANSFERASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR42755; 3-DEOXY-MANNO-OCTULOSONATE CYTIDYLYLTRANSFERASE; 1.
DR   Pfam; PF04413; Glycos_transf_N; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 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_0000286455"
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;  53047 MW;  476C023C396CFCFA CRC64;
     MMLLYYALSF ILLPVYFIII LIRLLIGKED IRRIQERFAI GKHRQDDSLD FMQTSANKEE
     FKGDTSLRTT TYTLIREDEG LGSTYKLPLE ASDARRLIWI NAASIGESMV ALTLIHNISK
     RYPDVRFLVT SWTNSSAKIL TAKLPKIAVH QFLPIDNIIF TRKFLRNWQP DLGIFIESEL
     WPCTINEGAK QCKLLLVNAR ISDKSFKAWL QRKSFFQLIL KNCSKIIVQS ERDLQKFNEL
     GVSDAVNLGN IKFANEKLPV NQEELSKLSL HLDNKRVVLF ASTHPEDEEV ILPIIKNLKE
     QFLDCYIILI PRHPERVKSI IDNCKSHNLS ATAKSQNDLP VLSDDLYIVD RFGEMGLFFS
     VATISFIGGS FKQGGHNILE AAYFSNCIIF GPDMSKNTDI AKGVLQNEAA IQIKNGEDLL
     TKLTYLLRSN NALELTTYRE NALKFIKDNQ KVLDEYLNVI TKFL
//