ID KDKA_STRMK Reviewed; 249 AA.
AC B2FR65;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=Smlt1004;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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=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: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; AM743169; CAQ44567.1; -; Genomic_DNA.
DR RefSeq; WP_012479275.1; NC_010943.1.
DR AlphaFoldDB; B2FR65; -.
DR SMR; B2FR65; -.
DR EnsemblBacteria; CAQ44567; CAQ44567; Smlt1004.
DR GeneID; 61464920; -.
DR KEGG; sml:Smlt1004; -.
DR PATRIC; fig|522373.3.peg.971; -.
DR eggNOG; COG3642; Bacteria.
DR HOGENOM; CLU_094226_0_0_6; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000008840; 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; Cell inner membrane; Cell membrane; Kinase;
KW Lipopolysaccharide biosynthesis; Membrane; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..249
FT /note="3-deoxy-D-manno-octulosonic acid kinase"
FT /id="PRO_1000200652"
FT ACT_SITE 175
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00521"
SQ SEQUENCE 249 AA; 28446 MW; BC5CFC19EA7D7D1B CRC64;
MVAFDANEAL TPCREGRGIG AILFDRERLR QAEVGLFSPQ HWGSKARPVG EGGRGSAWFI
DAPFGASVLR HYLRGGLAAK ISHDQYLWRG SDRTRSFAEF RLMRALREKK LPVPRPIAAY
YMREGLRYRA AILMERIEGV RSLADRALVA GRGAPWEETG RLIARFHRAG LDHADLNAHN
ILFDGNGHGW LIDFDRGVIR IPATAWRERN LKRLLRSLIK LRGERSVEDV QKDYARLRRA
YDMAWNRGT
//
