KAIC_THEVB
ID KAIC_THEVB Reviewed; 518 AA.
AC Q79V60; Q8RR33;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Circadian clock protein kinase KaiC;
DE EC=2.7.11.1;
GN Name=kaiC; OrderedLocusNames=tlr0483;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], HEXAMERIZATION, AND ATP-BINDING.
RX PubMed=12622725; DOI=10.1046/j.1365-2443.2003.00633.x;
RA Hayashi F., Suzuki H., Iwase R., Uzumaki T., Miyake A., Shen J.-R.,
RA Imada K., Furukawa Y., Yonekura K., Namba K., Ishiura M.;
RT "ATP-induced hexameric ring structure of the cyanobacterial circadian clock
RT protein KaiC.";
RL Genes Cells 8:287-296(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [3]
RP STRUCTURE BY NMR OF 488-518 IN COMPLEX WITH 180-283 OF KAIA.
RX PubMed=15256595; DOI=10.1073/pnas.0403037101;
RA Vakonakis I., LiWang A.C.;
RT "Structure of the C-terminal domain of the clock protein KaiA in complex
RT with a KaiC-derived peptide: implications for KaiC regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10925-10930(2004).
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 (By similarity). {ECO:0000250}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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 (By
CC similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q79V60; Q79V62: kaiA; NbExp=12; IntAct=EBI-701595, EBI-701584;
CC Q79V60; Q79V61: kaiB; NbExp=6; IntAct=EBI-701595, EBI-7570699;
CC Q79V60; Q79V60: kaiC; NbExp=8; IntAct=EBI-701595, EBI-701595;
CC -!- DOMAIN: The KaiC domains mediate the interaction with KaiA.
CC {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KaiC family. {ECO:0000305}.
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DR EMBL; AB071375; BAB85985.1; -; Genomic_DNA.
DR EMBL; BA000039; BAC08035.1; -; Genomic_DNA.
DR RefSeq; NP_681273.1; NC_004113.1.
DR RefSeq; WP_011056334.1; NC_004113.1.
DR PDB; 1SUY; NMR; -; C/D=488-518.
DR PDB; 1SV1; NMR; -; C/D=488-518.
DR PDB; 4O0M; X-ray; 2.84 A; A/B/C=1-518.
DR PDB; 5JWO; X-ray; 1.80 A; A=17-247.
DR PDB; 5JWQ; X-ray; 3.87 A; A/C=1-518.
DR PDB; 5JWR; X-ray; 2.61 A; A/C=17-247.
DR PDB; 6X61; X-ray; 3.20 A; A/C/E/G/I/K=17-247.
DR PDBsum; 1SUY; -.
DR PDBsum; 1SV1; -.
DR PDBsum; 4O0M; -.
DR PDBsum; 5JWO; -.
DR PDBsum; 5JWQ; -.
DR PDBsum; 5JWR; -.
DR PDBsum; 6X61; -.
DR AlphaFoldDB; Q79V60; -.
DR SMR; Q79V60; -.
DR DIP; DIP-29357N; -.
DR IntAct; Q79V60; 2.
DR MINT; Q79V60; -.
DR STRING; 197221.22294204; -.
DR EnsemblBacteria; BAC08035; BAC08035; BAC08035.
DR KEGG; tel:tlr0483; -.
DR PATRIC; fig|197221.4.peg.508; -.
DR eggNOG; COG0467; Bacteria.
DR OMA; MGSHSIT; -.
DR OrthoDB; 271085at2; -.
DR EvolutionaryTrace; Q79V60; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016301; F:kinase activity; IDA: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; IDA: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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Biological rhythms; DNA-binding; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Serine/threonine-protein kinase;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..518
FT /note="Circadian clock protein kinase KaiC"
FT /id="PRO_0000217779"
FT DOMAIN 20..260
FT /note="KaiC 1"
FT DOMAIN 261..493
FT /note="KaiC 2"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 288..295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 432
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:5JWO"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:5JWO"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:5JWO"
FT HELIX 53..68
FT /evidence="ECO:0007829|PDB:5JWO"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:5JWO"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:5JWO"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:5JWO"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:5JWO"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:5JWO"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:5JWR"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:4O0M"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:5JWO"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:5JWO"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:5JWO"
FT HELIX 158..174
FT /evidence="ECO:0007829|PDB:5JWO"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:5JWO"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:5JWR"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:5JWR"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:5JWR"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:5JWO"
FT STRAND 216..225
FT /evidence="ECO:0007829|PDB:5JWO"
FT STRAND 234..246
FT /evidence="ECO:0007829|PDB:5JWO"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:4O0M"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:4O0M"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:4O0M"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:4O0M"
FT HELIX 294..307
FT /evidence="ECO:0007829|PDB:4O0M"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:4O0M"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:4O0M"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:4O0M"
FT HELIX 335..340
FT /evidence="ECO:0007829|PDB:4O0M"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:4O0M"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:4O0M"
FT HELIX 356..370
FT /evidence="ECO:0007829|PDB:4O0M"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:4O0M"
FT TURN 381..386
FT /evidence="ECO:0007829|PDB:4O0M"
FT HELIX 389..405
FT /evidence="ECO:0007829|PDB:4O0M"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:4O0M"
FT STRAND 435..445
FT /evidence="ECO:0007829|PDB:4O0M"
FT STRAND 448..458
FT /evidence="ECO:0007829|PDB:4O0M"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:4O0M"
FT STRAND 476..482
FT /evidence="ECO:0007829|PDB:4O0M"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:1SUY"
FT HELIX 512..515
FT /evidence="ECO:0007829|PDB:1SV1"
SQ SEQUENCE 518 AA; 57538 MW; 34E4CDF9DE9C1824 CRC64;
MTNLPEHQSS PTEQSSAEVK KIPTMIEGFD DISHGGLPQG RTTLVSGTSG TGKTLFAVQF
LYNGITIFNE PGIFVTFEES PQDIIKNALS FGWNLQSLID QGKLFILDAS PDPDGQEVAG
DFDLSALIER IQYAIRKYKA TRVSIDSVTA VFQQYDAASV VRREIFRLAF RLKQLGVTTI
MTTERVDEYG PVARFGVEEF VSDNVVILRN VLEGERRRRT VEILKLRGTT HMKGEYPFTI
NNGINIFPLG AMRLTQRSSN VRVSSGVKTL DEMCGGGFFK DSIILATGAT GTGKTLLVSK
FLETGCQQGE RALLFAYEES RAQLSRNASS WGIDFEELER RGLLRIICAY PESAGLEDHL
QIIKSEIADF KPSRVAIDSL SALARGVSNN AFRQFVIGVT GFAKQEEITG FFTNTTDQFM
GSNSITESHI STITDTILLL QYVEIRGEMS RAINVFKMRG SWHDKGIREY VITEKGAEIR
DSFRNFEGII SGTPTRISVD EKTELARIAK GMQDLESE
