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   03-AUG-2022, entry version 70.
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; Proteobacteria; 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=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; AM743169; CAQ44567.1; -; Genomic_DNA.
DR   RefSeq; WP_012479275.1; NC_010943.1.
DR   AlphaFoldDB; B2FR65; -.
DR   SMR; B2FR65; -.
DR   STRING; 522373.Smlt1004; -.
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   OMA; YYRGGLW; -.
DR   OrthoDB; 1643499at2; -.
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   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;
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