ID G0CFH1_XANCA Unreviewed; 249 AA.
AC G0CFH1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
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=XCR_1193 {ECO:0000313|EMBL:AEL06096.1};
OS Xanthomonas campestris pv. raphani 756C.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=990315 {ECO:0000313|EMBL:AEL06096.1, ECO:0000313|Proteomes:UP000001633};
RN [1] {ECO:0000313|EMBL:AEL06096.1, ECO:0000313|Proteomes:UP000001633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=756C {ECO:0000313|EMBL:AEL06096.1,
RC ECO:0000313|Proteomes:UP000001633};
RX PubMed=21784931; DOI=10.1128/JB.05262-11;
RA Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., Patil P.B.,
RA Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., Aparna G., Rajaram M.,
RA Delcher A.L., Phillippy A.M., Puiu D., Schatz M.C., Shumway M.,
RA Sommer D.D., Trapnell C., Benahmed F., Dimitrov G., Madupu R., Radune D.,
RA Sullivan S., Jha G., Ishihara H., Lee S.W., Pandey A., Sharma V.,
RA Sriariyanun M., Szurek B., Vera-Cruz C.M., Dorman K.S., Ronald P.C.,
RA Verdier V., Dow J.M., Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D.,
RA Leach J.E., White F.F., Salzberg S.L.;
RT "Two new complete genome sequences offer insight into host and tissue
RT specificity of plant pathogenic Xanthomonas spp.";
RL J. Bacteriol. 193:5450-5464(2011).
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; CP002789; AEL06096.1; -; Genomic_DNA.
DR RefSeq; WP_011036197.1; NC_017271.1.
DR AlphaFoldDB; G0CFH1; -.
DR SMR; G0CFH1; -.
DR DNASU; 1001509; -.
DR GeneID; 58014431; -.
DR KEGG; xcp:XCR_1193; -.
DR PATRIC; fig|990315.4.peg.1121; -.
DR HOGENOM; CLU_094226_0_0_6; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000001633; 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:AEL06096.1};
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 ACT_SITE 175
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00521"
SQ SEQUENCE 249 AA; 28651 MW; CAE651318FF170C4 CRC64;
MVSFDATEAL TPYREGRGYG AILFDRERLR QADAGLFSPQ RWGDRARPVD EGGRGGAWFV
DAPFGHSVLR QYRRGGMAAR VSRDQYLWKG AGRTRSFAEF RLMRELLKRK LPVPRPLAAC
YLREGLGYRA ALLMERLENV RSLADHAQVA GRGAPWEDTG RLIARFHRAG LDHADLNAHN
ILFDAGGHGW LIDFDRGVLR IPATRWRERN LARLHRSLLK LRGNRTREDV DKDYERLHRA
YELAWGRGY
//
