ID   KDKA_VIBPA              Reviewed;         238 AA.
AC   Q87T74;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
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}; OrderedLocusNames=VP0196;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC58459.1; -; Genomic_DNA.
DR   RefSeq; NP_796575.1; NC_004603.1.
DR   RefSeq; WP_005459670.1; NC_004603.1.
DR   AlphaFoldDB; Q87T74; -.
DR   SMR; Q87T74; -.
DR   STRING; 223926.28805178; -.
DR   EnsemblBacteria; BAC58459; BAC58459; BAC58459.
DR   GeneID; 1187663; -.
DR   KEGG; vpa:VP0196; -.
DR   PATRIC; fig|223926.6.peg.188; -.
DR   eggNOG; COG3642; Bacteria.
DR   HOGENOM; CLU_094226_0_0_6; -.
DR   OMA; YYRGGLW; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   HAMAP; MF_00521; KDO_kinase; 1.
DR   InterPro; IPR022826; KDO_kinase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..238
FT                   /note="3-deoxy-D-manno-octulosonic acid kinase"
FT                   /id="PRO_0000194317"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00521"
SQ   SEQUENCE   238 AA;  27695 MW;  AD100C0FB4EA4217 CRC64;
     MIQQYRDSNQ VIWFDEELIE DPSQPIFDAE YWQSTNKVTG SASGRGTTWF VQLDTMQAAL
     RHYRRGGLFG KLVKDNYLFS GWEQTRCAQE FQLLLTLINA GVHVPRPIAA RAVKSGLTYQ
     ADLLSERIPN ARDLVSILQE KPLPEGMYQK IGQEIAKMHN AGVNHTDLNI HNILIDDKDK
     VWIIDFDKCR KQEHGDWKKQ NLERLLRSFK KELLKRQIHW KERDFAVLTE ALSCLDIK