KAIC_SYNY3
ID KAIC_SYNY3 Reviewed; 519 AA.
AC P74646;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=slr0758;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Core component of the KaiABC clock protein complex, which
CC constitutes the main circadian regulator in cyanobacteria. Binds to
CC DNA. The KaiABC 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 -!- ACTIVITY REGULATION: The interaction with KaiA enhances its
CC phosphorylation status, while the interaction with KaiB decreases it. A
CC KaiA dimer is sufficient to enhance KaiC phosphorylation.
CC {ECO:0000255|HAMAP-Rule:MF_01836}.
CC -!- SUBUNIT: Homohexamer; hexamerization is dependent on ATP-binding. Core
CC component of the KaiABC complex, at least composed of a KaiC
CC homohexamer, a KaiB dimer and two KaiA dimers. Interacts directly with
CC SasA. {ECO:0000255|HAMAP-Rule:MF_01836}.
CC -!- DOMAIN: The KaiC domains mediate the interaction with KaiA.
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; BA000022; BAA18762.1; -; Genomic_DNA.
DR PIR; S76850; S76850.
DR AlphaFoldDB; P74646; -.
DR SMR; P74646; -.
DR IntAct; P74646; 2.
DR STRING; 1148.1653852; -.
DR PaxDb; P74646; -.
DR EnsemblBacteria; BAA18762; BAA18762; BAA18762.
DR KEGG; syn:slr0758; -.
DR eggNOG; COG0467; Bacteria.
DR InParanoid; P74646; -.
DR OMA; MGSHSIT; -.
DR PhylomeDB; P74646; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISS:UniProtKB.
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; TAS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
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..519
FT /note="Circadian clock protein kinase KaiC"
FT /id="PRO_0000217786"
FT DOMAIN 20..261
FT /note="KaiC 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT DOMAIN 262..494
FT /note="KaiC 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 289..296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 320
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT MOD_RES 433
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
SQ SEQUENCE 519 AA; 58294 MW; 799DE04C94BF416F CRC64;
MNLPIVNERN RPDVPRKGVQ KIRTVIEGFD EITHGGLPIG RTTLVSGTSG TGKTLLAVQF
LYQGIHHFDY PGLFITFEES PSDIIENAYS FGWDLQQLID DGKLFILDAS PDPEGQEVVG
TFDLSALIER IQYAVRKYKA KLVSIDSVTA VFQQYDAASV VRREIFRLVA RLKQLQVTSI
MTTERVEEYG PIARFGVEEF VSDNVVVLRN VLEGERRRRT VEILKLRGTT HMKGEYPFTI
THDGINIFPL GAMRLTQRSS NARISSGVQT LDEMCGGGFF KDSIILATGA TGTGKTLLVS
KFLQEGCRQR ERAILFAYEE SRAQLSRNAS SWGIDFEEME HKGLLKLLCT YPESAGLEDH
LQMIKSEISE FKPSRIAIDS LSALARGVTN NAFRQFVIGV TGYAKQEEIT GFFTNTTDQF
MGAHSITESH ISTITDTILM LQYVEIRGEM SRALNVFKMR GSWHDKGIRE YSISHDGPDI
RDSFRNYERI ISGSPTRISV DEKSELSRIV RGVKDKTAE
