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Database: UniProt
Entry: A0A0R2BYJ9_9LACO
LinkDB: A0A0R2BYJ9_9LACO
Original site: A0A0R2BYJ9_9LACO 
ID   A0A0R2BYJ9_9LACO        Unreviewed;       132 AA.
AC   A0A0R2BYJ9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=(d)CMP kinase {ECO:0000256|ARBA:ARBA00012906};
DE            EC=2.7.4.25 {ECO:0000256|ARBA:ARBA00012906};
GN   ORFNames=FD21_GL002178 {ECO:0000313|EMBL:KRM84080.1};
OS   Liquorilactobacillus vini DSM 20605.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1133569 {ECO:0000313|EMBL:KRM84080.1, ECO:0000313|Proteomes:UP000051576};
RN   [1] {ECO:0000313|EMBL:KRM84080.1, ECO:0000313|Proteomes:UP000051576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20605 {ECO:0000313|EMBL:KRM84080.1,
RC   ECO:0000313|Proteomes:UP000051576};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001097};
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001115};
CC   -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009427}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRM84080.1}.
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DR   EMBL; AYYX01000096; KRM84080.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2BYJ9; -.
DR   STRING; 1133569.FD21_GL002178; -.
DR   PATRIC; fig|1133569.4.peg.2345; -.
DR   eggNOG; COG0283; Bacteria.
DR   Proteomes; UP000051576; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   CDD; cd02020; CMPK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003136; Cytidylate_kin.
DR   InterPro; IPR011994; Cytidylate_kinase_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00017; cmk; 1.
DR   PANTHER; PTHR21299:SF2; CYTIDYLATE KINASE; 1.
DR   PANTHER; PTHR21299; CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE; 1.
DR   Pfam; PF02224; Cytidylate_kin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:KRM84080.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051576};
KW   Transferase {ECO:0000313|EMBL:KRM84080.1}.
FT   DOMAIN          2..126
FT                   /note="Cytidylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF02224"
SQ   SEQUENCE   132 AA;  14640 MW;  1E1D177B21A1AD52 CRC64;
     MSKYVSTVAA QISVREALTA KQQKLAVNGG IVMDGRDIGT TVLPNAQVKI FLVASVKERA
     LRRYREDVAK GFKVDLQQLE SEIALRDKKD ESRAISPLTQ AEDAILVDTT SLSIEQVVEK
     IMKIIKKEVK RA
//
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