KAIC_PROMA
ID KAIC_PROMA Reviewed; 501 AA.
AC Q7VAN5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Circadian clock protein kinase KaiC {ECO:0000255|HAMAP-Rule:MF_01836};
DE EC=2.7.11.1 {ECO:0000255|HAMAP-Rule:MF_01836};
GN Name=kaiC {ECO:0000255|HAMAP-Rule:MF_01836}; OrderedLocusNames=Pro_1423;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
CC -!- FUNCTION: Core component of the KaiBC clock protein complex, which
CC constitutes the main circadian regulator in cyanobacteria. Binds to
CC DNA. The KaiBC complex may act as a promoter-nonspecific transcription
CC regulator that represses transcription, possibly by acting on the state
CC of chromosome compaction. {ECO:0000255|HAMAP-Rule:MF_01836}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01836};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000255|HAMAP-Rule:MF_01836};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01836};
CC -!- SUBUNIT: Homohexamer; hexamerization is dependent on ATP-binding.
CC Component of the KaiBC complex with KaiB. Interacts directly with SasA.
CC {ECO:0000255|HAMAP-Rule:MF_01836}.
CC -!- PTM: Phosphorylated on serine/threonine residues by autocatalysis. Both
CC phosphorylated and unphosphorylated forms exist. Can probably
CC autophosphorylate and autodephosphorylate. Phosphorylated form
CC correlates with clock speed. {ECO:0000255|HAMAP-Rule:MF_01836}.
CC -!- SIMILARITY: Belongs to the KaiC family. {ECO:0000255|HAMAP-
CC Rule:MF_01836}.
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DR EMBL; AE017126; AAQ00467.1; -; Genomic_DNA.
DR RefSeq; NP_875814.1; NC_005042.1.
DR RefSeq; WP_011125574.1; NC_005042.1.
DR AlphaFoldDB; Q7VAN5; -.
DR SMR; Q7VAN5; -.
DR STRING; 167539.Pro_1423; -.
DR PRIDE; Q7VAN5; -.
DR EnsemblBacteria; AAQ00467; AAQ00467; Pro_1423.
DR GeneID; 54200760; -.
DR KEGG; pma:Pro_1423; -.
DR PATRIC; fig|167539.5.peg.1489; -.
DR eggNOG; COG0467; Bacteria.
DR HOGENOM; CLU_023669_4_1_3; -.
DR OMA; MGSHSIT; -.
DR OrthoDB; 271085at2; -.
DR Proteomes; UP000001420; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007623; P:circadian rhythm; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0042752; P:regulation of circadian rhythm; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_01836; KaiC; 1.
DR InterPro; IPR013503; Circadian_KaiC_bact.
DR InterPro; IPR030665; KaiC.
DR InterPro; IPR014774; KaiC-like_dom.
DR InterPro; IPR010624; KaiC_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF06745; ATPase; 2.
DR PIRSF; PIRSF039117; KaiC; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR02655; circ_KaiC; 1.
DR PROSITE; PS51146; KAIC; 2.
PE 3: Inferred from homology;
KW ATP-binding; Biological rhythms; DNA-binding; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Serine/threonine-protein kinase; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..501
FT /note="Circadian clock protein kinase KaiC"
FT /id="PRO_0000217776"
FT DOMAIN 4..245
FT /note="KaiC 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT DOMAIN 246..478
FT /note="KaiC 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 273..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT MOD_RES 417
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
SQ SEQUENCE 501 AA; 55906 MW; DC0FF241D8C4E9BA CRC64;
MQVQKLPTGI EGFDDVCQGG LPTARSTLVS GTSGTGKTVF SLQYLHHGIC HFDEPGVFVT
FEESPLDIIR NAGSFGWDLQ ELINQDKLFV LDASPDPDGQ DVAGNFDLSG LIERISYAIK
KYKAKRVAID SMTAVFQQYD AVYVVRREIF RLIARLKEIG VTTVMTSERI DEYGPIARYG
VEEFVSDNVV ILRNVLESEK RRRTVEVLKL RGTTHMKGEF PFTMGAEGIT VFALGAMRLT
QRSSNIRISS GVPDLDDMCG GGYFQDSIIL ATGATGTGKT MLVSKFIEDA YRNQERAIIF
AYEESRAQLL RNATSWGIDF EQMEADGLLK IICAYPESTG LEDHLQIIKT EITEFKPSRM
AIDSLSALAR GVSLNAFRQF VIGVTGYAKQ EEIAGFFTNT AEEFMGSHSI TDSHISTITD
TILLLQYVEI RGEMARAINV FKMRGSWHDK RIREFIITNE GPEIKDSFTN FEQIFSGAPH
RISGEDSISG VFKSLDKREK K
