ID   KDTA_RICBR              Reviewed;         418 AA.
AC   Q1RGU8;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=RBE_1335;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE05416.1; -; Genomic_DNA.
DR   RefSeq; WP_011477985.1; NC_007940.1.
DR   AlphaFoldDB; Q1RGU8; -.
DR   SMR; Q1RGU8; -.
DR   STRING; 336407.RBE_1335; -.
DR   CAZy; GT30; Glycosyltransferase Family 30.
DR   EnsemblBacteria; ABE05416; ABE05416; RBE_1335.
DR   KEGG; rbe:RBE_1335; -.
DR   eggNOG; COG1519; Bacteria.
DR   HOGENOM; CLU_036146_2_0_5; -.
DR   OMA; FIKYEFW; -.
DR   OrthoDB; 1163086at2; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000001951; 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; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..418
FT                   /note="3-deoxy-D-manno-octulosonic acid transferase"
FT                   /id="PRO_0000286454"
FT   TRANSMEM        7..27
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         264..265
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250"
FT   BINDING         305..307
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250"
FT   BINDING         330..333
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250"
FT   SITE            130
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            205
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   418 AA;  48119 MW;  3819786AA9570F63 CRC64;
     MMRLYYFLSF LLLPIYFVII FIRLLIGKED IRRVKERFAI GKHRQDNRFL IWIHAASVGE
     SMIALNLVDN ISKHFPEVRF LVTSWTQSSA KILSTKLPKI ATHQLLPIDN IIFTKIFLNN
     WKPDLGIFIE SELWPGTINE AAKQCNLLLV NARMSDKSFE SWKKRKGFFQ LIVKNFSEVI
     VQSERDLQKF NELGISNTTN LGNIKFANEK LPVNQEELIK LSEHLKNKQV ILFASTHPED
     EEIILPIIKN LKKQVIDCYI ILIPRHPERI KSILDNCIAQ DLSATAKSQN DLPVLTDDLY
     IVDRFGEMGL FFSIASISFI GGSFKQGGHN ILEAAHFSNC IIFGPDMSKN TDIAKGVLQS
     KAAIQIKSGE ELLNMLEYLL DPNNSRELKN YQENSLKFVE RNQKILDEYL QIITKFFP