ID   KDKA_XYLFM              Reviewed;         249 AA.
AC   B0U358;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Xfasm12_1357;
OS   Xylella fastidiosa (strain M12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405440;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M12;
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}.
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; CP000941; ACA12287.1; -; Genomic_DNA.
DR   RefSeq; WP_012337922.1; NC_010513.1.
DR   AlphaFoldDB; B0U358; -.
DR   KEGG; xfm:Xfasm12_1357; -.
DR   HOGENOM; CLU_094226_0_0_6; -.
DR   OMA; YYRGGLW; -.
DR   OrthoDB; 1643499at2; -.
DR   UniPathway; UPA00958; -.
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_1000127648"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00521"
SQ   SEQUENCE   249 AA;  28831 MW;  31A31AA507DAEF5A CRC64;
     MVAFDANEIL TPFCEGHREG AILFDCQRMR QVEYGLFVPA WWGERAHPVS EGGRGSAWFV
     EASFGNAVLR QYRRGGMIAM LNRDRYFWCG GHRTRSVLEF RLMRELISRG LPVPTPLAAC
     YVRYGVQYRA AILIERLEGV SSLAMCIRGN SKETHWEQIG RMISRFHREG LDHADLNAHN
     ILLDPAGQCW LIDFDRGALR IPATKWRERN LARLLRSLLK IRGERSVDAV YRDFERLRRA
     YDLAWSRGC