ID   KDKA_VIBCH              Reviewed;         235 AA.
AC   Q9KVB9;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=3-deoxy-D-manno-octulosonic acid kinase;
DE            Short=Kdo kinase;
DE            EC=2.7.1.166;
GN   Name=kdkA; OrderedLocusNames=VC_0227;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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:0000250}.
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   -!- 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 protein kinase superfamily. KdkA/RfaP
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF93403.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE003852; AAF93403.1; ALT_INIT; Genomic_DNA.
DR   PIR; E82348; E82348.
DR   RefSeq; NP_229884.1; NC_002505.1.
DR   RefSeq; WP_000616620.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KVB9; -.
DR   SMR; Q9KVB9; -.
DR   STRING; 243277.VC_0227; -.
DR   DNASU; 2614177; -.
DR   EnsemblBacteria; AAF93403; AAF93403; VC_0227.
DR   GeneID; 57738963; -.
DR   KEGG; vch:VC_0227; -.
DR   PATRIC; fig|243277.26.peg.208; -.
DR   eggNOG; COG3642; Bacteria.
DR   HOGENOM; CLU_094226_0_0_6; -.
DR   OMA; YYRGGLW; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000000584; 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..235
FT                   /note="3-deoxy-D-manno-octulosonic acid kinase"
FT                   /id="PRO_0000194316"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   235 AA;  27408 MW;  66B26A78E58625DF CRC64;
     MIQTFNDAQQ KVWFDDALLH EDPSQCCNPE FWQQNGKVLG SATGRGTTWF VQLQQTQGAL
     RHYRRGGLFG KLVADSYWFT GWEKTRSYQE FMLLNHLRDA GVNVPRPIAA RVQKHGLLYK
     ADLLSEKVPN ARDLVSILQE SPISDELYRK IGREIRKMHD AQVNHTDLNI HNILIDDQEK
     VWIIDFDKCY VQIGDSWKQG NLKRLKRSFE KEVCKRGINW SLEAFAIISS YKHEE