ID   URK_STRPN               Reviewed;         212 AA.
AC   P67413; Q97QJ7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Uridine kinase {ECO:0000255|HAMAP-Rule:MF_00551};
DE            EC=2.7.1.48 {ECO:0000255|HAMAP-Rule:MF_00551};
DE   AltName: Full=Cytidine monophosphokinase {ECO:0000255|HAMAP-Rule:MF_00551};
DE   AltName: Full=Uridine monophosphokinase {ECO:0000255|HAMAP-Rule:MF_00551};
GN   Name=udk {ECO:0000255|HAMAP-Rule:MF_00551}; OrderedLocusNames=SP_1208;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + uridine = ADP + H(+) + UMP; Xref=Rhea:RHEA:16825,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57865, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00551};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00551};
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC       CTP from cytidine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00551}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       UMP from uridine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00551}.
CC   -!- INTERACTION:
CC       P67413; P15057: CPL1; Xeno; NbExp=2; IntAct=EBI-11615933, EBI-11615908;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00551}.
CC   -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00551}.
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DR   EMBL; AE005672; AAK75315.1; -; Genomic_DNA.
DR   PIR; B95140; B95140.
DR   RefSeq; WP_001181378.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; P67413; -.
DR   SMR; P67413; -.
DR   IntAct; P67413; 1.
DR   STRING; 170187.SP_1208; -.
DR   EnsemblBacteria; AAK75315; AAK75315; SP_1208.
DR   GeneID; 60233216; -.
DR   GeneID; 66806324; -.
DR   KEGG; spn:SP_1208; -.
DR   eggNOG; COG0572; Bacteria.
DR   OMA; TTLKPMH; -.
DR   PhylomeDB; P67413; -.
DR   BioCyc; SPNE170187:G1FZB-1224-MON; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0004849; F:uridine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd02023; UMPK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00551; Uridine_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006083; PRK/URK.
DR   InterPro; IPR026008; Uridine_kinase.
DR   InterPro; IPR000764; Uridine_kinase-like.
DR   Pfam; PF00485; PRK; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00235; udk; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..212
FT                   /note="Uridine kinase"
FT                   /id="PRO_0000164499"
FT   BINDING         12..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00551"
SQ   SEQUENCE   212 AA;  24466 MW;  47B405D377C70A8A CRC64;
     MQNRPIIIGV TGGSGGGKTS VSRAILSHFP DEKISMIEHD SYYKDQSHLT FEERVKTNYD
     HPFAFDTDLM IEQIKELLAG RPVDIPTYDY TEHTRSSKTY RQEPQDVFIV EGILVLEDKR
     LRDLMDIKIF VDTDDDVRII RRIKRDMEER GRSLDSVINQ YLGVVKPMYH QFIESTKRYA
     DIVIPEGVSN TVAIDLLTTK IAKILEEARN SK