KDKA_XANC5
ID KDKA_XANC5 Reviewed; 249 AA.
AC Q3BWM9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=3-deoxy-D-manno-octulosonic acid kinase {ECO:0000255|HAMAP-Rule:MF_00521};
DE Short=Kdo kinase {ECO:0000255|HAMAP-Rule:MF_00521};
DE EC=2.7.1.166 {ECO:0000255|HAMAP-Rule:MF_00521};
GN Name=kdkA {ECO:0000255|HAMAP-Rule:MF_00521}; OrderedLocusNames=XCV1103;
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10;
RX PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT genome sequence.";
RL J. Bacteriol. 187:7254-7266(2005).
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:0000255|HAMAP-Rule:MF_00521}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Kdo-(2->6)-lipid IVA + ATP = 4-O-phospho-alpha-Kdo-
CC (2->6)-lipid IVA + ADP + H(+); Xref=Rhea:RHEA:28506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:60364,
CC ChEBI:CHEBI:61589, ChEBI:CHEBI:456216; EC=2.7.1.166;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00521};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00521}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00521}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00521}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00521}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. KdkA/RfaP
CC family. {ECO:0000255|HAMAP-Rule:MF_00521}.
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DR EMBL; AM039952; CAJ22734.1; -; Genomic_DNA.
DR RefSeq; WP_011346602.1; NZ_CP017190.1.
DR AlphaFoldDB; Q3BWM9; -.
DR SMR; Q3BWM9; -.
DR STRING; 456327.BJD11_17160; -.
DR EnsemblBacteria; CAJ22734; CAJ22734; XCV1103.
DR KEGG; xcv:XCV1103; -.
DR eggNOG; COG3642; Bacteria.
DR HOGENOM; CLU_094226_0_0_6; -.
DR OMA; YYRGGLW; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000007069; 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 HAMAP; MF_00521; KDO_kinase; 1.
DR InterPro; IPR022826; KDO_kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW Lipopolysaccharide biosynthesis; Membrane; Nucleotide-binding; Transferase.
FT CHAIN 1..249
FT /note="3-deoxy-D-manno-octulosonic acid kinase"
FT /id="PRO_0000263416"
FT ACT_SITE 175
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00521"
SQ SEQUENCE 249 AA; 28407 MW; 1928FEA878F6193F CRC64;
MVSFDATEAL APYREGRGYG AILFDRERLR QADASLFSPQ SWGDRARPVD AGGRGGAWFV
DAPFGHSVLR QYLRGGMAAR VSRDRYLWKG AGRTRSFAEF RLMRELIKRK LPVPRPLAAC
YLREGVGYRA ALLMERLENV RSLADHAQVA GRGAPWEATG QLIARFHRAG LDHADLNAHN
ILFDAGGHGW LIDFDRGVLR IPATRWRERN LKRLHRSLLK LRGNRSREDV DKDYARLHRA
YELAWGRGY