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Circadian clock protein kinase KaiC (EC 2.7.11.1)

 KAIC_THEEB              Reviewed;         518 AA.
Q79V60; Q8RR33;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
28-FEB-2018, entry version 99.
RecName: Full=Circadian clock protein kinase KaiC;
EC=2.7.11.1;
Name=kaiC; OrderedLocusNames=tlr0483;
Thermosynechococcus elongatus (strain BP-1).
Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
Thermosynechococcus.
NCBI_TaxID=197221;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], HEXAMERIZATION, AND ATP-BINDING.
PubMed=12622725; DOI=10.1046/j.1365-2443.2003.00633.x;
Hayashi F., Suzuki H., Iwase R., Uzumaki T., Miyake A., Shen J.-R.,
Imada K., Furukawa Y., Yonekura K., Namba K., Ishiura M.;
"ATP-induced hexameric ring structure of the cyanobacterial circadian
clock protein KaiC.";
Genes Cells 8:287-296(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BP-1;
PubMed=12240834; DOI=10.1093/dnares/9.4.123;
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
"Complete genome structure of the thermophilic cyanobacterium
Thermosynechococcus elongatus BP-1.";
DNA Res. 9:123-130(2002).
[3]
STRUCTURE BY NMR OF 488-518 IN COMPLEX WITH 180-283 OF KAIA.
PubMed=15256595; DOI=10.1073/pnas.0403037101;
Vakonakis I., LiWang A.C.;
"Structure of the C-terminal domain of the clock protein KaiA in
complex with a KaiC-derived peptide: implications for KaiC
regulation.";
Proc. Natl. Acad. Sci. U.S.A. 101:10925-10930(2004).
-!- FUNCTION: Core component of the KaiABC clock protein complex,
which constitutes the main circadian regulator in cyanobacteria.
Binds to DNA. The KaiABC complex may act as a promoter-nonspecific
transcription regulator that represses transcription, possibly by
acting on the state of chromosome compaction (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: The interaction with KaiA enhances its
phosphorylation status, while the interaction with KaiB decreases
it. A KaiA dimer is sufficient to enhance KaiC phosphorylation (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Homohexamer; hexamerization is dependent on ATP-binding.
Core component of the KaiABC complex, at least composed of a KaiC
homohexamer, a KaiB dimer and two KaiA dimers. Interacts directly
with SasA (By similarity). {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=8; IntAct=EBI-701595, EBI-701595;
Q79V62:kaiA; NbExp=12; IntAct=EBI-701595, EBI-701584;
Q79V61:kaiB; NbExp=6; IntAct=EBI-701595, EBI-7570699;
-!- DOMAIN: The KaiC domains mediate the interaction with KaiA.
{ECO:0000250}.
-!- PTM: Phosphorylated on serine/threonine residues by autocatalysis.
Both phosphorylated and unphosphorylated forms exist. Can probably
autophosphorylate and autodephosphorylate. Phosphorylated form
correlates with clock speed (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the KaiC family. {ECO:0000305}.
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EMBL; AB071375; BAB85985.1; -; Genomic_DNA.
EMBL; BA000039; BAC08035.1; -; Genomic_DNA.
RefSeq; NP_681273.1; NC_004113.1.
RefSeq; WP_011056334.1; NC_004113.1.
PDB; 1SUY; NMR; -; C/D=488-518.
PDB; 1SV1; NMR; -; C/D=488-518.
PDB; 4O0M; X-ray; 2.84 A; A/B/C=1-518.
PDB; 5JWO; X-ray; 1.80 A; A=17-247.
PDB; 5JWQ; X-ray; 3.87 A; A/C=1-518.
PDB; 5JWR; X-ray; 2.61 A; A/C=17-247.
PDBsum; 1SUY; -.
PDBsum; 1SV1; -.
PDBsum; 4O0M; -.
PDBsum; 5JWO; -.
PDBsum; 5JWQ; -.
PDBsum; 5JWR; -.
ProteinModelPortal; Q79V60; -.
SMR; Q79V60; -.
DIP; DIP-29357N; -.
IntAct; Q79V60; 2.
MINT; Q79V60; -.
STRING; 197221.tlr0483; -.
EnsemblBacteria; BAC08035; BAC08035; BAC08035.
GeneID; 1012389; -.
KEGG; tel:tlr0483; -.
PATRIC; fig|197221.4.peg.508; -.
eggNOG; ENOG4105EHU; Bacteria.
eggNOG; COG0467; LUCA.
HOGENOM; HOG000230416; -.
KO; K08482; -.
OMA; HSITDSH; -.
OrthoDB; POG091H0SAA; -.
BioCyc; TELO197221:G1G3I-497-MONOMER; -.
EvolutionaryTrace; Q79V60; -.
Proteomes; UP000000440; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0007623; P:circadian rhythm; TAS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; IEA:InterPro.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
HAMAP; MF_01836; KaiC; 1.
InterPro; IPR013503; Circadian_KaiC_bact.
InterPro; IPR030665; KaiC.
InterPro; IPR014774; KaiC-like_dom.
InterPro; IPR010624; KaiC_dom.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF06745; ATPase; 2.
PIRSF; PIRSF039117; KaiC; 1.
SUPFAM; SSF52540; SSF52540; 2.
TIGRFAMs; TIGR02655; circ_KaiC; 1.
PROSITE; PS51146; KAIC; 2.
1: Evidence at protein level;
3D-structure; ATP-binding; Biological rhythms; Complete proteome;
DNA-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
Phosphoprotein; Reference proteome; Repeat; Repressor;
Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase.
CHAIN 1 518 Circadian clock protein kinase KaiC.
/FTId=PRO_0000217779.
DOMAIN 20 260 KaiC 1.
DOMAIN 261 493 KaiC 2.
NP_BIND 47 54 ATP. {ECO:0000250}.
NP_BIND 288 295 ATP. {ECO:0000250}.
METAL 295 295 Magnesium. {ECO:0000250}.
METAL 318 318 Magnesium. {ECO:0000250}.
METAL 319 319 Magnesium. {ECO:0000250}.
METAL 378 378 Magnesium. {ECO:0000250}.
MOD_RES 432 432 Phosphothreonine; by autocatalysis.
{ECO:0000250}.
HELIX 29 32 {ECO:0000244|PDB:5JWO}.
STRAND 35 38 {ECO:0000244|PDB:5JWO}.
STRAND 41 46 {ECO:0000244|PDB:5JWO}.
HELIX 53 68 {ECO:0000244|PDB:5JWO}.
STRAND 72 79 {ECO:0000244|PDB:5JWO}.
HELIX 81 88 {ECO:0000244|PDB:5JWO}.
HELIX 89 91 {ECO:0000244|PDB:5JWO}.
HELIX 95 100 {ECO:0000244|PDB:5JWO}.
STRAND 103 108 {ECO:0000244|PDB:5JWO}.
STRAND 116 118 {ECO:0000244|PDB:5JWR}.
STRAND 119 122 {ECO:0000244|PDB:4O0M}.
HELIX 125 138 {ECO:0000244|PDB:5JWO}.
STRAND 142 146 {ECO:0000244|PDB:5JWO}.
HELIX 148 154 {ECO:0000244|PDB:5JWO}.
HELIX 158 174 {ECO:0000244|PDB:5JWO}.
STRAND 178 183 {ECO:0000244|PDB:5JWO}.
STRAND 188 190 {ECO:0000244|PDB:5JWR}.
HELIX 194 196 {ECO:0000244|PDB:5JWR}.
TURN 197 200 {ECO:0000244|PDB:5JWR}.
STRAND 205 213 {ECO:0000244|PDB:5JWO}.
STRAND 216 225 {ECO:0000244|PDB:5JWO}.
STRAND 234 246 {ECO:0000244|PDB:5JWO}.
TURN 249 251 {ECO:0000244|PDB:4O0M}.
HELIX 268 273 {ECO:0000244|PDB:4O0M}.
STRAND 276 281 {ECO:0000244|PDB:4O0M}.
STRAND 283 289 {ECO:0000244|PDB:4O0M}.
HELIX 294 307 {ECO:0000244|PDB:4O0M}.
STRAND 312 319 {ECO:0000244|PDB:4O0M}.
HELIX 321 329 {ECO:0000244|PDB:4O0M}.
TURN 330 332 {ECO:0000244|PDB:4O0M}.
HELIX 335 340 {ECO:0000244|PDB:4O0M}.
STRAND 343 348 {ECO:0000244|PDB:4O0M}.
HELIX 351 353 {ECO:0000244|PDB:4O0M}.
HELIX 356 370 {ECO:0000244|PDB:4O0M}.
STRAND 373 378 {ECO:0000244|PDB:4O0M}.
TURN 381 386 {ECO:0000244|PDB:4O0M}.
HELIX 389 405 {ECO:0000244|PDB:4O0M}.
STRAND 409 415 {ECO:0000244|PDB:4O0M}.
STRAND 435 445 {ECO:0000244|PDB:4O0M}.
STRAND 448 458 {ECO:0000244|PDB:4O0M}.
STRAND 468 473 {ECO:0000244|PDB:4O0M}.
STRAND 476 482 {ECO:0000244|PDB:4O0M}.
HELIX 506 508 {ECO:0000244|PDB:1SUY}.
HELIX 512 515 {ECO:0000244|PDB:1SV1}.
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


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