ID G7G062_9GAMM Unreviewed; 242 AA.
AC G7G062;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:GAA78785.1};
GN ORFNames=P20495_1279 {ECO:0000313|EMBL:GAA78785.1};
OS Pseudoalteromonas sp. BSi20495.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=386429 {ECO:0000313|EMBL:GAA78785.1, ECO:0000313|Proteomes:UP000003050};
RN [1] {ECO:0000313|Proteomes:UP000003050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSi20495 {ECO:0000313|Proteomes:UP000003050};
RX PubMed=22275105; DOI=10.1128/JB.06427-11;
RA Bian F., Xie B.B., Qin Q.L., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA Chen X.L., Zhou B.C., Zhang Y.Z.;
RT "Genome sequences of six Pseudoalteromonas strains isolated from Arctic sea
RT ice.";
RL J. Bacteriol. 194:908-909(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:GAA78785.1}.
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DR EMBL; BADY01000041; GAA78785.1; -; Genomic_DNA.
DR RefSeq; WP_008134925.1; NZ_BADY01000041.1.
DR AlphaFoldDB; G7G062; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000003050; 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:GAA78785.1};
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, ECO:0000313|EMBL:GAA78785.1}.
FT DOMAIN 1..242
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 167
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00521"
SQ SEQUENCE 242 AA; 27879 MW; 37ED79727F6A470B CRC64;
MFKQHVQGNH TVLSHPKYTS QITLDWFDAN YWQQQNKIVG AKKGRATAWF FKQDELTAVL
RHYWRGGLVG KLLSDQYLYL GLEQTRVYKE FSLMSKLIEL GLNVPTPVAA KVTHSGLIYR
GDIITEAVKG AKSVLDILIE RPLTEDELER IAKTIALFHS KGVYHADLNI NNILFNDTGD
VYIIDFDRGE IRAPNPQWQQ SNMARLERSF LKEQGRNKPF NWQASDWQTL HSNYLKALAN
IS
//
