ID G0GE44_SPITZ Unreviewed; 800 AA.
AC G0GE44;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=Spith_1125 {ECO:0000313|EMBL:AEJ61397.1};
OS Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=869211 {ECO:0000313|EMBL:AEJ61397.1, ECO:0000313|Proteomes:UP000007254};
RN [1] {ECO:0000313|EMBL:AEJ61397.1, ECO:0000313|Proteomes:UP000007254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700085 / DSM 6578 / Z-1203
RC {ECO:0000313|Proteomes:UP000007254};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikailova N., Pagani I.,
RA Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Merkhoffer B., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Spirochaeta thermophila DSM 6578.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002903; AEJ61397.1; -; Genomic_DNA.
DR AlphaFoldDB; G0GE44; -.
DR STRING; 869211.Spith_1125; -.
DR KEGG; stq:Spith_1125; -.
DR HOGENOM; CLU_015805_1_1_12; -.
DR OrthoDB; 9804077at2; -.
DR Proteomes; UP000007254; 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:0003676; F:nucleic acid binding; IEA:InterPro.
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 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; IPR035104; Ribosomal_protein_S1-like.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00017; cmk; 1.
DR PANTHER; PTHR10724; 30S RIBOSOMAL PROTEIN S1; 1.
DR PANTHER; PTHR10724:SF13; 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:AEJ61397.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00238};
KW Reference proteome {ECO:0000313|Proteomes:UP000007254};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00238}.
FT DOMAIN 262..323
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 341..409
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 430..498
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 515..585
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 602..672
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 689..761
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT BINDING 8..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00238"
SQ SEQUENCE 800 AA; 91465 MW; 35F3A8D557020C2E CRC64;
MMIIAIDGPA GVGKSTVARC IAERLHLPHV NSGDLYRAVT YLAIMAQYLS PLREEAIILL
ARDLTCRIVE GVLDIDGIPS LSELHTDQVD RWVAQVSSLP EVRNHVTEKL RTLVRESGGV
VEGRDIGTVV FPDTPYKFFL DATPEERARR RFLQGTSSLP YEELVKEIRR RDEIDRNKPL
GALKQAPGAV YIDTSDLTSE AVCEKVIQII RQISENRSRT DMMNHQNSTL DPQMNTSPDP
SVPEQEELQE IYLKTLEEVE EGSLVEGTVI EINKDYVYLD VGYKSEGQVP ISDFDTLPKV
GDTVPVVILR KETADGHILV SKKKADQRLF WKTLKDAFQE KKPIEGKIVR EIKGGFEVDL
GHGFSGFLPR SQTDIERVED VSPYIGLETR FLIERLFSNR KVNIVLSRRR WLEEERERKR
TEFFETRKEG DIVEGVVKSF APFGAFIDLG GFDGLLHLQD MSWGRAVRPK DYVKKGEKVR
VKIIKMDREQ QKVNLSLKAL KEDPWTHFEE RYHRGDVVEG VVTKLMPFGA FVEIEEGIEG
LVHISEMSWV KTIEHPKEVL KRGARIQAKI LDYDIEERRL SLGIRQLQAN PWETLHERYP
VGMRLTRPIT QIFPHGAVVE LEEGIEAFLP AENISWTERV EDVTTLFQPG QEIEFCITRI
DKKRRRIQIG IKQLSEDPWK ALAKAFPEGS EIETKILRKE PQGIVVEVQG GIEGFIPNRQ
LCDPAVETPE NVRDRLKEGD TIRALVLELK PSKRRLILSI REKERKEQER ELSKYLHEGE
GETTFSIADL LSSSQEDESE
//
