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Database: UniProt
Entry: R1GQC1_9GAMM
LinkDB: R1GQC1_9GAMM
Original site: R1GQC1_9GAMM 
ID   R1GQC1_9GAMM            Unreviewed;       234 AA.
AC   R1GQC1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=G113_17168 {ECO:0000313|EMBL:EOD53900.1};
OS   Aeromonas molluscorum 848.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=1268236 {ECO:0000313|EMBL:EOD53900.1, ECO:0000313|Proteomes:UP000013526};
RN   [1] {ECO:0000313|EMBL:EOD53900.1, ECO:0000313|Proteomes:UP000013526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=848 {ECO:0000313|EMBL:EOD53900.1,
RC   ECO:0000313|Proteomes:UP000013526};
RX   PubMed=23788549;
RA   Spataro N., Farfan M., Albarral V., Sanglas A., Loren J.G., Fuste M.C.,
RA   Bosch E.;
RT   "Draft Genome Sequence of Aeromonas molluscorum Strain 848TT, Isolated from
RT   Bivalve Molluscs.";
RL   Genome Announc. 1:E00382-13(2013).
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:EOD53900.1}.
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DR   EMBL; AQGQ01000155; EOD53900.1; -; Genomic_DNA.
DR   RefSeq; WP_005907402.1; NZ_AQGQ01000155.1.
DR   AlphaFoldDB; R1GQC1; -.
DR   PATRIC; fig|1268236.3.peg.3355; -.
DR   OrthoDB; 6854449at2; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000013526; 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:EOD53900.1};
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          36..234
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00521"
SQ   SEQUENCE   234 AA;  26875 MW;  AE7FE8AC5F4DD228 CRC64;
     MQIQTDKNQV CWFADELFNN PSPRLFDPVW WQNQGKVVGS AIGRGVTWFV KEESCHLVLR
     HYYRGGMVGR VVRDRFWFEG VESSRAMAEF SLLDTLSRQG LPVPRPFGAR MVKQGPFYRA
     DILIERIRGA KDLVALLKRG PVAAEIWLGV GQAIRRLHDA GVYHADLNSH NLLLDKADKV
     WVIDFDKGAI RAPGSWQQAN LERLLRSFNK EAQLHTSFHF VPENWQTLMQ GYRG
//
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