KCY_STRPN
ID KCY_STRPN Reviewed; 223 AA.
AC Q97PK6;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cytidylate kinase {ECO:0000255|HAMAP-Rule:MF_00238};
DE Short=CK {ECO:0000255|HAMAP-Rule:MF_00238};
DE EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00238};
DE AltName: Full=Cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00238};
DE Short=CMP kinase {ECO:0000255|HAMAP-Rule:MF_00238};
GN Name=cmk {ECO:0000255|HAMAP-Rule:MF_00238}; OrderedLocusNames=SP_1603;
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 + CMP = ADP + CDP; Xref=Rhea:RHEA:11600,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00238};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593,
CC ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00238};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00238}.
CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00238}.
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DR EMBL; AE005672; AAK75687.1; -; Genomic_DNA.
DR PIR; F95186; F95186.
DR RefSeq; WP_000849381.1; NZ_AKVY01000001.1.
DR PDB; 1Q3T; NMR; -; A=1-223.
DR PDBsum; 1Q3T; -.
DR AlphaFoldDB; Q97PK6; -.
DR SMR; Q97PK6; -.
DR STRING; 170187.SP_1603; -.
DR EnsemblBacteria; AAK75687; AAK75687; SP_1603.
DR KEGG; spn:SP_1603; -.
DR eggNOG; COG0283; Bacteria.
DR OMA; RAITWWM; -.
DR PhylomeDB; Q97PK6; -.
DR BioCyc; SPNE170187:G1FZB-1624-MON; -.
DR EvolutionaryTrace; Q97PK6; -.
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:0036430; F:CMP kinase activity; IEA:RHEA.
DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd02020; CMPK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00238; Cytidyl_kinase_type1; 1.
DR InterPro; IPR003136; Cytidylate_kin.
DR InterPro; IPR011994; Cytidylate_kinase_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02224; Cytidylate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00017; cmk; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..223
FT /note="Cytidylate kinase"
FT /id="PRO_0000131985"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00238"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1Q3T"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:1Q3T"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1Q3T"
FT HELIX 34..47
FT /evidence="ECO:0007829|PDB:1Q3T"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:1Q3T"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1Q3T"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:1Q3T"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:1Q3T"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1Q3T"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:1Q3T"
FT HELIX 106..120
FT /evidence="ECO:0007829|PDB:1Q3T"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1Q3T"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:1Q3T"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1Q3T"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:1Q3T"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:1Q3T"
FT HELIX 170..184
FT /evidence="ECO:0007829|PDB:1Q3T"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1Q3T"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:1Q3T"
FT HELIX 208..222
FT /evidence="ECO:0007829|PDB:1Q3T"
SQ SEQUENCE 223 AA; 24597 MW; EDE12AD6B4D721DC CRC64;
MKTIQIAIDG PASSGKSTVA KIIAKDFGFT YLDTGAMYRA ATYMALKNQL GVEEVEALLA
LLDQHPISFG RSETGDQLVF VGDVDITHPI RENEVTNHVS AIAAIPQVRE KLVSLQQEIA
QQGGIVMDGR DIGTVVLPQA ELKIFLVASV DERAERRYKE NIAKGIETDL ETLKKEIAAR
DYKDSHRETS PLKQAEDAVY LDTTGLNIQE VVEKIKAEAE KRM
