ID   KDKA_PHOPR              Reviewed;         236 AA.
AC   Q6LVM6;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=PBPRA0210;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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; CR378663; CAG18649.1; -; Genomic_DNA.
DR   RefSeq; WP_011217025.1; NC_006370.1.
DR   AlphaFoldDB; Q6LVM6; -.
DR   STRING; 298386.PBPRA0210; -.
DR   EnsemblBacteria; CAG18649; CAG18649; PBPRA0210.
DR   KEGG; ppr:PBPRA0210; -.
DR   eggNOG; COG3642; Bacteria.
DR   HOGENOM; CLU_094226_0_0_6; -.
DR   OMA; YYRGGLW; -.
DR   OrthoDB; 1643499at2; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000000593; 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: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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..236
FT                   /note="3-deoxy-D-manno-octulosonic acid kinase"
FT                   /id="PRO_0000263414"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00521"
SQ   SEQUENCE   236 AA;  27063 MW;  5D4A2D1998386EA6 CRC64;
     MEELCFDNQR IWFDPNLLQE DPKACFDASF WQQQGKVIGS AQGRGTTWFV QGETLPMALR
     HYRRGGLFGK LIEDAYVFTG WEKTRCAEEV ALLSTLAVGG VNVPRPVAAR ATRHGLVYRA
     DLLVEKIDSA KDLVDLLQQA MLPDHVWYAI GRTVRKMHDL QVCHTDLNAH NILVDSRELV
     WLIDFDKCYT QEGEAWKAKN LSRLHRSFVK EQGKRNIHFS ATSWQVLCQG YELPDN