ID F5YHW7_TREPZ Unreviewed; 798 AA.
AC F5YHW7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Cytidylate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE Short=CK {ECO:0000256|HAMAP-Rule:MF_00238};
DE EC=2.7.4.25 {ECO:0000256|HAMAP-Rule:MF_00238};
DE AltName: Full=Cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE Short=CMP kinase {ECO:0000256|HAMAP-Rule:MF_00238};
GN Name=cmk {ECO:0000256|HAMAP-Rule:MF_00238};
GN OrderedLocusNames=TREPR_2339 {ECO:0000313|EMBL:AEF83765.1};
OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF83765.1, ECO:0000313|Proteomes:UP000009223};
RN [1] {ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA Paulsen I.T.;
RT "Complete sequence of Treponema primitia strain ZAS-2.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF83765.1, ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RX PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT spirochete species in co-culture.";
RL ISME J. 5:1133-1142(2011).
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, ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00001115, ECO:0000256|HAMAP-
CC Rule:MF_00238};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000256|ARBA:ARBA00006767}.
CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009427, ECO:0000256|HAMAP-Rule:MF_00238}.
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DR EMBL; CP001843; AEF83765.1; -; Genomic_DNA.
DR RefSeq; WP_015707864.1; NC_015578.1.
DR AlphaFoldDB; F5YHW7; -.
DR STRING; 545694.TREPR_2339; -.
DR KEGG; tpi:TREPR_2339; -.
DR eggNOG; COG0539; Bacteria.
DR HOGENOM; CLU_015805_1_1_12; -.
DR OrthoDB; 9804077at2; -.
DR Proteomes; UP000009223; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd02020; CMPK; 1.
DR CDD; cd05687; S1_RPS1_repeat_ec1_hs1; 1.
DR CDD; cd04465; S1_RPS1_repeat_ec2_hs2; 1.
DR CDD; cd05688; S1_RPS1_repeat_ec3; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 6.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00238; Cytidyl_kinase_type1; 1.
DR InterPro; IPR003136; Cytidylate_kin.
DR InterPro; IPR011994; Cytidylate_kinase_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000110; Ribosomal_bS1.
DR InterPro; IPR035104; Ribosomal_protein_S1-like.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00017; cmk; 1.
DR NCBIfam; TIGR00717; rpsA; 1.
DR PANTHER; PTHR10724; 30S RIBOSOMAL PROTEIN S1; 1.
DR Pfam; PF02224; Cytidylate_kin; 1.
DR Pfam; PF00575; S1; 6.
DR PRINTS; PR00681; RIBOSOMALS1.
DR SMART; SM00316; S1; 6.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 6.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50126; S1; 6.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00238};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00238, ECO:0000313|EMBL:AEF83765.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00238};
KW Reference proteome {ECO:0000313|Proteomes:UP000009223};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000313|EMBL:AEF83765.1};
KW Ribosomal protein {ECO:0000313|EMBL:AEF83765.1};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00238}.
FT DOMAIN 260..321
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 339..407
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 428..496
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 513..583
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 600..670
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 687..759
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 214..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00238"
SQ SEQUENCE 798 AA; 89217 MW; 218C692D812B6390 CRC64;
MIIAIDGPAG SGKSTIAKLL AEGLKYTYVN SGNLYRAITL GCLRNHIDPL DQTAALAYAE
SADIEYRDGD VYLAGENVVS LLHTDEIDQF TAPLSANVPI RHVVNRLIRK IAGKLDVVVE
GRDMTTVVFP KAEHRFYLDA TPEARAKRRL DQGVSKLSFE EILKTIQERD EIDKNKTEGS
LKIGPGVLVF DTSVLTISQV YERLIEEIQR KGSTMGQMEV ESDTSPIDES NGITSANTGD
DIQTQLQEKY LKSLEQLEEG QLVDGHVIQV TPDQVFVDVG YKSEGKIPIA EFTEIPQVGD
TVSVILVAKE NKHGEVIVSK QKADVKLFWK NLRQGFQDHT MVEGTIEKLV KGGYDVDLGA
GVRAFLPISQ SDAQKVDKPE KLLGLKTNFY VERLYSDGKV NIVVNRRKWL EEEIEQKRKD
FFEKTQIGDD ITGEVKSFTS FGAFIDLGGF DGLLHINDMS WGHVTRPKDF VKKGQEIRLK
VIRIDPQEKR INLSLKHFTD DPWVHFEDKY HVNDVIKGKV TKLTDFGAFV ELEEGIEGLV
HISEFSWVKK IQKPEELLSI GDETECMILG YDLQAGRVSL GLKQVTANPW TGIEERYPLG
TRLTRKVAKI TNAGAFIELE DGIDGFLHGD DISWTKKVKH PGSEFAAGQE IEVMVISIDP
ENKNIRLGIK QLSEDPWQSF ASAYKPGSLV EGEVSSVTDF GIFVRIPGGI EGLIHKSNLP
ENREDNPDEL LKKYQIGDKI KAVVLELQPD KQKVAFSIKD YQKKVQRDEI SQYMAAEESD
GSTFTLGDFL KSKNTPEG
//
