ID   KDKA_XYLF2              Reviewed;         249 AA.
AC   B2I5R8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=3-deoxy-D-manno-octulosonic acid kinase {ECO:0000255|HAMAP-Rule:MF_00521};
DE            Short=Kdo kinase {ECO:0000255|HAMAP-Rule:MF_00521};
DE            EC=2.7.1.166 {ECO:0000255|HAMAP-Rule:MF_00521};
GN   Name=kdkA {ECO:0000255|HAMAP-Rule:MF_00521};
GN   OrderedLocusNames=XfasM23_1292;
OS   Xylella fastidiosa (strain M23).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405441;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M23;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(2010).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of the 3-deoxy-D-
CC       manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at the 4-OH
CC       position. {ECO:0000255|HAMAP-Rule:MF_00521}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-Kdo-(2->6)-lipid IVA + ATP = 4-O-phospho-alpha-Kdo-
CC         (2->6)-lipid IVA + ADP + H(+); Xref=Rhea:RHEA:28506,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:60364,
CC         ChEBI:CHEBI:61589, ChEBI:CHEBI:456216; EC=2.7.1.166;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00521};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00521}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00521}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00521}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00521}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. KdkA/RfaP
CC       family. {ECO:0000255|HAMAP-Rule:MF_00521}.
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DR   EMBL; CP001011; ACB92713.1; -; Genomic_DNA.
DR   RefSeq; WP_004088627.1; NC_010577.1.
DR   AlphaFoldDB; B2I5R8; -.
DR   EnsemblBacteria; ACB92713; ACB92713; XfasM23_1292.
DR   GeneID; 58016751; -.
DR   KEGG; xfn:XfasM23_1292; -.
DR   HOGENOM; CLU_094226_0_0_6; -.
DR   OMA; YYRGGLW; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000001698; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   HAMAP; MF_00521; KDO_kinase; 1.
DR   InterPro; IPR022826; KDO_kinase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   SUPFAM; SSF56112; SSF56112; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW   Lipopolysaccharide biosynthesis; Membrane; Nucleotide-binding; Transferase.
FT   CHAIN           1..249
FT                   /note="3-deoxy-D-manno-octulosonic acid kinase"
FT                   /id="PRO_1000127647"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00521"
SQ   SEQUENCE   249 AA;  28764 MW;  5BE5683AAC7D1489 CRC64;
     MVAFDANEIL TPFCEGHREG AILFDCQRMR QVEYGLFVPA WWGERAHPIS EGGRGSAWFV
     EASFGNAVLR QYRRGGMIAM LNRDRYFWCG GHRTRSVLEF RLMRELISRG LPVPTPLAAC
     YVRHGVQYRA AILMERLEGV SSLAMCVRGN SKEIHWEQIG RMISRFHREG LDHADLNAHN
     ILLDQAGQCW LIDFDRGALR IPATKWREHN LARLLRSLLK IRGERSVDAV YRDFERLCRA
     YDLAWGRGC