ID   KDTA_BORPT              Reviewed;         428 AA.
AC   Q45374;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=3-deoxy-D-manno-octulosonic acid transferase;
DE            Short=Kdo transferase;
DE            EC=2.4.99.12 {ECO:0000269|PubMed:10198035};
DE   AltName: Full=Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase;
DE   AltName: Full=Monofunctional Kdo transferase;
GN   Name=waaA;
OS   Bordetella pertussis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=520;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BP536;
RX   PubMed=8821935; DOI=10.1046/j.1365-2958.1996.354877.x;
RA   Allen A.G., Maskell D.J.;
RT   "The identification, cloning and mutagenesis of a genetic locus required
RT   for lipopolysaccharide biosynthesis in Bordetella pertussis.";
RL   Mol. Microbiol. 19:37-52(1996).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=BP536;
RX   PubMed=10198035; DOI=10.1128/jb.181.8.2648-2651.1999;
RA   Isobe T., White K.A., Allen A.G., Peacock M., Raetz C.R., Maskell D.J.;
RT   "Bordetella pertussis waaA encodes a monofunctional 2-keto-3-deoxy-D-manno-
RT   octulosonic acid transferase that can complement an Escherichia coli waaA
RT   mutation.";
RL   J. Bacteriol. 181:2648-2651(1999).
CC   -!- FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes
CC       the transfer of a single 3-deoxy-D-manno-octulosonate (Kdo) residue
CC       from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-
CC       bisphosphate precursor of lipid A. {ECO:0000269|PubMed:10198035}.
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         Evidence={ECO:0000269|PubMed:10198035};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
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; X90711; CAA62243.1; -; Genomic_DNA.
DR   PIR; S70670; S70670.
DR   RefSeq; WP_010929616.1; NZ_UIGD01000005.1.
DR   AlphaFoldDB; Q45374; -.
DR   SMR; Q45374; -.
DR   CAZy; GT30; Glycosyltransferase Family 30.
DR   GeneID; 45387502; -.
DR   OMA; FIKYEFW; -.
DR   OrthoDB; 1163086at2; -.
DR   UniPathway; UPA00958; -.
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; IPR001296; Glyco_trans_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; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF04413; Glycos_transf_N; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Lipopolysaccharide biosynthesis;
KW   Membrane; Transferase.
FT   CHAIN           1..428
FT                   /note="3-deoxy-D-manno-octulosonic acid transferase"
FT                   /id="PRO_0000419172"
FT   ACT_SITE        64
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         274..275
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250"
FT   BINDING         316..318
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250"
FT   BINDING         342..345
FT                   /ligand="CMP"
FT                   /ligand_id="ChEBI:CHEBI:60377"
FT                   /evidence="ECO:0000250"
FT   SITE            137
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            213
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   428 AA;  45462 MW;  79652087C50140D8 CRC64;
     MGRGVYTLAL RGLAPLIWLW MWRRARRAGG QWELFAPARF GRAGARAPAP LAAPVWVHAV
     SLGETRAAQP LVQALLERGL PVLLTHTTAT GRAEGERLFG AAIGRGQLQQ AWLPYDFPGA
     TRRFLARHAP RCGLLMEREV WPNLLAAARA QGVPMALVSA RFSASSLRQA GWLGQALREA
     LAGLDRVLAQ TDEDGARLCQ AGANAYTVTG SLKFDVALPE AQLRVGHAWA GATGRPVIAL
     ASTREGEDAM FIEAIGALQA HRAATPRPLI LLIPRHPQRF DEAAAQLQAA GLAYARRSAG
     SGEPGPHIDV LLGDTLGEMP FYYAAADVAI VGGSFARLGG QNLIEACAAG TPVIVGPHTF
     NFKDAARDAI AAGAALRAPD ARTALDWALQ LLAEPARRQA MSEAARAWTA AHAGATRRTL
     DALEDWLG