KDKA_VIBVY
ID KDKA_VIBVY Reviewed; 236 AA.
AC Q7MPR5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=VV0297;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(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; BA000037; BAC93061.1; -; Genomic_DNA.
DR RefSeq; WP_011149270.1; NC_005139.1.
DR AlphaFoldDB; Q7MPR5; -.
DR SMR; Q7MPR5; -.
DR STRING; 672.VV93_v1c02880; -.
DR EnsemblBacteria; BAC93061; BAC93061; BAC93061.
DR KEGG; vvy:VV0297; -.
DR PATRIC; fig|196600.6.peg.331; -.
DR eggNOG; COG3642; Bacteria.
DR HOGENOM; CLU_094226_0_0_6; -.
DR OMA; YYRGGLW; -.
DR OrthoDB; 1643499at2; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000002675; Chromosome I.
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_0000194319"
FT ACT_SITE 167
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00521"
SQ SEQUENCE 236 AA; 27508 MW; 1C9C4BB00B392E28 CRC64;
MIEQQQFGQS RICYDSEWVS SPELALFDPQ YWQAQNKVVG SATGRGTTWF VQLPKITAAL
RHYRRGGLFG KLVKDHYWFR SWSATRSFAE FHLLKQLREA GVNVPRPIAA YAMRKGLFYQ
ADLLSERIAN AQDLVTILQK HSLNAELYQK IGVEIAKMHR VGVNHTDLNI HNILIDAQET
IWIIDFDKCY PQAGDGWKQE NLDRLKRSFN KERVKRSIHW HDKDFQALLT GYESQQ