KAIC_NOSS1
ID KAIC_NOSS1 Reviewed; 519 AA.
AC Q8YT40;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=alr2886;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
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=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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; AB071284; BAB85869.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB74585.1; -; Genomic_DNA.
DR PIR; AG2166; AG2166.
DR RefSeq; WP_010997037.1; NZ_RSCN01000003.1.
DR AlphaFoldDB; Q8YT40; -.
DR SMR; Q8YT40; -.
DR STRING; 103690.17131980; -.
DR EnsemblBacteria; BAB74585; BAB74585; BAB74585.
DR KEGG; ana:alr2886; -.
DR eggNOG; COG0467; Bacteria.
DR OMA; MGSHSIT; -.
DR OrthoDB; 271085at2; -.
DR Proteomes; UP000002483; 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..519
FT /note="Circadian clock protein kinase KaiC"
FT /id="PRO_0000217775"
FT DOMAIN 18..259
FT /note="KaiC 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT DOMAIN 260..492
FT /note="KaiC 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 287..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 377
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT MOD_RES 431
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
SQ SEQUENCE 519 AA; 57920 MW; 59D456D89F6CCA20 CRC64;
MSEKEQQEQQ NTSGNGVEKI RTMIEGFDDI SHGGLPVGRT TLVSGTSGTG KTLLSLQFLF
NGISFFDEPG VFVTFEESPS DIIKNAHIFG WNLQRLINEG KLFILDASPD PEGQDIVGNF
DLSALIERLQ YAIRKYKAKR VSIDSITAVF QQYEAVGVVR REIFRLVARL KQLNVTTIIT
TERSEEYGPV ASFGVEEFVS DNVVIARNVL EGERRRRTIE ILKLRGTTHM KGEYPFTITN
DGVNIFPLGA MRLTQRSSNV RVSSGVKTLD GMCGGGFFKD SIILATGATG TGKTLLVSKF
LQNGCVNNER AILFAYEESR AQLSRNAYSW GIDFEELESQ GLLKIICTYP ESTGLEDHLQ
IIKSEIAYFK PARIAIDSLS ALARGVSNNA FRQFVIGVTG YAKQEEITGF FTNTTDQFMG
SHSITDSHIS TITDTILMLQ YVEIRGEMSR AINVFKMRGS WHDKGIREYN ITADGPEIQD
SFRNYERIVS GSPTRVSIDE KAELSRIVRR FEDKQGSDS
