ID A0A2N8ZGQ5_9VIBR Unreviewed; 237 AA.
AC A0A2N8ZGQ5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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 ECO:0000313|EMBL:SON51067.1};
GN ORFNames=VTAP4600_A3101 {ECO:0000313|EMBL:SON51067.1};
OS Vibrio tapetis subsp. tapetis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1671868 {ECO:0000313|EMBL:SON51067.1, ECO:0000313|Proteomes:UP000235828};
RN [1] {ECO:0000313|EMBL:SON51067.1, ECO:0000313|Proteomes:UP000235828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vibrio tapetis CECT4600 {ECO:0000313|EMBL:SON51067.1};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; LT960611; SON51067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N8ZGQ5; -.
DR KEGG; vta:A3101; -.
DR OrthoDB; 6854449at2; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000235828; Chromosome a.
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 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 Pfam; PF06293; Kdo; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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:SON51067.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000235828};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00521, ECO:0000313|EMBL:SON51067.1}.
FT ACT_SITE 167
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00521"
SQ SEQUENCE 237 AA; 27570 MW; 61C73AD68B90ED89 CRC64;
MLQSIESHKQ IIWYDASFIM NPTSEHFDGE YWQRLGKVVG SAQGRGTTWF VQLEEMQAAL
RHYRRGGLFG KLVKDHYWFA GWENTRCYQE LLLLKHLRES GVNVPRPIAA IAKKRTICYQ
ADILSEKIVN ARDLVSILQD SSLSVETYNS IGEQIRLMHN AGVNHTDLNI HNILLDSEHK
VWIIDFDKCA KQDGEKWKAA NLERLLRSFN KELNKRAIRW QQSEWGALLV GYRSNKI
//
