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Database: UniProt
Entry: C9QDH7_VIBOR
LinkDB: C9QDH7_VIBOR
Original site: C9QDH7_VIBOR 
ID   C9QDH7_VIBOR            Unreviewed;       239 AA.
AC   C9QDH7;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=3-deoxy-D-manno-octulosonic acid kinase {ECO:0000256|ARBA:ARBA00029511, ECO:0000256|HAMAP-Rule:MF_00521};
DE            Short=Kdo kinase {ECO:0000256|HAMAP-Rule:MF_00521};
DE            EC=2.7.1.166 {ECO:0000256|ARBA:ARBA00011988, ECO:0000256|HAMAP-Rule:MF_00521};
GN   Name=kdkA {ECO:0000256|HAMAP-Rule:MF_00521};
GN   ORFNames=VIOR3934_06544 {ECO:0000313|EMBL:EGU52140.1};
OS   Vibrio orientalis CIP 102891 = ATCC 33934.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=675816 {ECO:0000313|EMBL:EGU52140.1, ECO:0000313|Proteomes:UP000002817};
RN   [1] {ECO:0000313|EMBL:EGU52140.1, ECO:0000313|Proteomes:UP000002817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 102891 / ATCC 33934 {ECO:0000313|Proteomes:UP000002817};
RX   PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA   Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA   McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT   "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT   Scleritoderma cyanea.";
RL   Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:0000256|HAMAP-Rule:MF_00521}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-Kdo-(2->6)-lipid IVA + ATP = a 4-O-phospho-alpha-Kdo-
CC         (2->6)-lipid IVA + ADP + H(+); Xref=Rhea:RHEA:74271,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:176428,
CC         ChEBI:CHEBI:193140, ChEBI:CHEBI:456216; EC=2.7.1.166;
CC         Evidence={ECO:0000256|ARBA:ARBA00034417, ECO:0000256|HAMAP-
CC         Rule:MF_00521};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004713, ECO:0000256|HAMAP-Rule:MF_00521}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00521}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00521}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00521}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. KdkA/RfaP
CC       family. {ECO:0000256|ARBA:ARBA00010327, ECO:0000256|HAMAP-
CC       Rule:MF_00521}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGU52140.1}.
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DR   EMBL; AFWH01000014; EGU52140.1; -; Genomic_DNA.
DR   RefSeq; WP_004410822.1; NZ_AFWH01000014.1.
DR   AlphaFoldDB; C9QDH7; -.
DR   STRING; 675816.VIA_000542; -.
DR   PATRIC; fig|675816.5.peg.1105; -.
DR   eggNOG; COG3642; Bacteria.
DR   OrthoDB; 6854449at2; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000002817; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   Pfam; PF06293; Kdo; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00521};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00521};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00521};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00521, ECO:0000313|EMBL:EGU52140.1};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00521};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00521};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00521};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00521}.
FT   DOMAIN          1..239
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00521"
SQ   SEQUENCE   239 AA;  27723 MW;  4276585AA403D356 CRC64;
     MFKQTQINNT TYWHDPLLLP ENVEQAFSIE YWQVNNAVTG SAQGRGTTWF VQGEQGEFAL
     RHYRRGGLFG KIIKDSYWFT SLEETRAYQE LKLLRQLIEC NVNVPVPVAA RATKSGLTYQ
     ADIIVQRISN ANDLVGLLSQ QVLSKELFKK VGWEVKKMHD ASVNHTDLNI HNILIDQSNQ
     VWIIDFDKCK REEIDNGWKQ SNLERLKRSF DKEVRLGKIQ LPDYAWTSLE EGYQSNENV
//
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