ID Q8E8I7_SHEON Unreviewed; 250 AA.
AC Q8E8I7;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 122.
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:AAN57636.1};
GN OrderedLocusNames=SO_4677 {ECO:0000313|EMBL:AAN57636.1};
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN57636.1, ECO:0000313|Proteomes:UP000008186};
RN [1] {ECO:0000313|EMBL:AAN57636.1, ECO:0000313|Proteomes:UP000008186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN57636.1,
RC ECO:0000313|Proteomes:UP000008186};
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN57636.1; -; Genomic_DNA.
DR RefSeq; NP_720192.1; NC_004347.2.
DR RefSeq; WP_011074268.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8E8I7; -.
DR STRING; 211586.SO_4677; -.
DR PaxDb; 211586-SO_4677; -.
DR DNASU; 1172259; -.
DR KEGG; son:SO_4677; -.
DR PATRIC; fig|211586.12.peg.4535; -.
DR eggNOG; COG0478; Bacteria.
DR HOGENOM; CLU_094226_0_0_6; -.
DR OrthoDB; 6854449at2; -.
DR BioCyc; MetaCyc:MONOMER-19352; -.
DR BioCyc; SONE211586:G1GMP-4324-MONOMER; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000008186; Chromosome.
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:AAN57636.1};
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:UP000008186};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00521, ECO:0000313|EMBL:AAN57636.1}.
FT ACT_SITE 170
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00521"
SQ SEQUENCE 250 AA; 28749 MW; BACC75167158E587 CRC64;
MNAQIKIINT ANGYMALCQD TPEDITPAWF SVDFWREKSA VVGSSKGRYT TWFVAFEHSH
WVLRHYWRGG MMEKFSKDAY FYTGLENTRA MGELRLLDAL YREQFAVPKP IAANIVRDGL
FYRADIIIER VDGAEDLVAK LTKGTMTQAQ WHALGATIAQ FHRRGVYHAD LNAKNILWQP
QQTDSAQERF YLIDFDRGEL KTPNAKWQKA NLDRLLRSFN KEQGKQPTLA FTPANWAALL
EGYHAVVPKV
//
