KDKA_STRM5
ID KDKA_STRM5 Reviewed; 249 AA.
AC B4SLP5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=Smal_0850;
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001111; ACF50555.1; -; Genomic_DNA.
DR RefSeq; WP_012510203.1; NC_011071.1.
DR AlphaFoldDB; B4SLP5; -.
DR SMR; B4SLP5; -.
DR STRING; 391008.Smal_0850; -.
DR EnsemblBacteria; ACF50555; ACF50555; Smal_0850.
DR KEGG; smt:Smal_0850; -.
DR eggNOG; COG3642; Bacteria.
DR HOGENOM; CLU_094226_0_0_6; -.
DR OMA; YYRGGLW; -.
DR OrthoDB; 1643499at2; -.
DR BioCyc; SMAL391008:SMAL_RS04395-MON; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000001867; 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_1000200653"
FT ACT_SITE 175
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00521"
SQ SEQUENCE 249 AA; 28472 MW; C7674D6AE5B3AC47 CRC64;
MVAFDANEAL TPCREGRGIG AILFDRERLR QAEADLFSPQ HWGSKARPVG EGGRGSAWFI
DAPFGASVLR HYLRGGLAAK ISHDQYLWRG ADRTRSFAEF RLMRALREKK LPVPRPLAAF
YMREGLRYRA AILMERIEGV RSLADRALVA GRGAPWEETG RLIARFHRAG LDHADLNAHN
ILFDGNGHGW LIDFDRGVIR IPATAWRERN LKRLLRSLIK LRGERSVEDV QKDYVRLRRA
YDMAWNRGT