KAIC_SYNP2
ID KAIC_SYNP2 Reviewed; 516 AA.
AC Q6L8L5; B1XMW0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 120.
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};
GN OrderedLocusNames=SYNPCC7002_A0287;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15170179; DOI=10.1038/nsmb781;
RA Uzumaki T., Fujita M., Nakatsu T., Hayashi F., Shibata H., Itoh N.,
RA Kato H., Ishiura M.;
RT "Crystal structure of the C-terminal clock-oscillator domain of the
RT cyanobacterial KaiA protein.";
RL Nat. Struct. Mol. Biol. 11:623-631(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; AB120711; BAD21213.1; -; Genomic_DNA.
DR EMBL; CP000951; ACA98297.1; -; Genomic_DNA.
DR RefSeq; WP_012305921.1; NC_010475.1.
DR AlphaFoldDB; Q6L8L5; -.
DR SMR; Q6L8L5; -.
DR STRING; 32049.SYNPCC7002_A0287; -.
DR EnsemblBacteria; ACA98297; ACA98297; SYNPCC7002_A0287.
DR KEGG; syp:SYNPCC7002_A0287; -.
DR eggNOG; COG0467; Bacteria.
DR HOGENOM; CLU_023669_4_1_3; -.
DR OMA; MGSHSIT; -.
DR Proteomes; UP000001688; 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..516
FT /note="Circadian clock protein kinase KaiC"
FT /id="PRO_0000217781"
FT DOMAIN 16..257
FT /note="KaiC 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT DOMAIN 258..490
FT /note="KaiC 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 285..292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 375
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT MOD_RES 429
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT CONFLICT 302
FT /note="G -> S (in Ref. 1; BAD21213)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 57440 MW; 3271F7A12B838ADC CRC64;
MNQPTSSNNG AIKGVQKIRT LIEGLDEISH GGLPSGRTTL VSGTSGTGKT LLAIQFLYHG
IKHFDYPGLF VTFEESPRDI IQNAHSFGWD LQSLVDEGKL FILDASPDPD GQEVVGNFDL
SALIERIQYA IRKYNAKLVS IDSVTAVFQQ YDAAPVVRRE IFRLVARLKH LAVTSIMTTE
RLDEYGPVAR FGVEEFVSDN VVILRNVLEG ERRRRTIEIL KLRGTTHMKG EYPFTITNDG
INIFPLGAMR LTQRSSNARI SSGVETLDKM CGGGFFKDSI ILATGATGTG KTLLVSKFLE
EGCRRGERAI LFAYEESRAQ LSRNASSWGI DFEEMERKGL LKLLCSYPES AGLEDHLQMI
KSEISEFKPS RIAIDSLSAL ARGVTNNAFR QFVIGVTGYA KQEEITGFFT NTTDQFMGAH
SITESHISTI TDTILMLQYV EIRGEMSRAI NVFKMRGSWH DKGIREYTIS EGGAAIKDSF
RNYERIISGS PTRIAVDEKS ELSRIMRGVQ DKTLPE
