KAIC_PARMW
ID KAIC_PARMW Reviewed; 512 AA.
AC Q7U8R3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=SYNW0550;
OS Parasynechococcus marenigrum (strain WH8102).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Parasynechococcus; Parasynechococcus marenigrum.
OX NCBI_TaxID=84588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8102;
RX PubMed=12917641; DOI=10.1038/nature01943;
RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT "The genome of a motile marine Synechococcus.";
RL Nature 424:1037-1042(2003).
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; BX569690; CAE07065.1; -; Genomic_DNA.
DR RefSeq; WP_011127419.1; NC_005070.1.
DR AlphaFoldDB; Q7U8R3; -.
DR SMR; Q7U8R3; -.
DR STRING; 84588.SYNW0550; -.
DR EnsemblBacteria; CAE07065; CAE07065; SYNW0550.
DR KEGG; syw:SYNW0550; -.
DR eggNOG; COG0467; Bacteria.
DR HOGENOM; CLU_023669_4_1_3; -.
DR OMA; MGSHSIT; -.
DR OrthoDB; 271085at2; -.
DR Proteomes; UP000001422; 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; Repeat; Repressor;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..512
FT /note="Circadian clock protein kinase KaiC"
FT /id="PRO_0000217784"
FT DOMAIN 15..256
FT /note="KaiC 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT DOMAIN 257..489
FT /note="KaiC 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 284..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT BINDING 314
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 374
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
FT MOD_RES 428
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01836"
SQ SEQUENCE 512 AA; 56970 MW; 6538C006584520BE CRC64;
MQFPPASGST QMQVQKLPTG IEGFDDVCQG GLPIGRSTLI SGTSGTGKTV FSLHFLHNGI
KHFDEPGIFV TFEESPLDIL RNAASFGWNL QEMVEQDKLF ILDASPDPDG QDVAGSFDLS
GLIERINYAI RKYKAKRVAI DSITAVFQQY DAVFVVRREI FRLIARLKEI GVTTVMTTER
IDEYGPIARY GVEEFVSDNV VILRNVLEGE RRRRTVEILK LRGTTHMKGE FPFTMGTHGI
SIFPLGAMRL TQRSSNVRVS SGVPRLDEMC GGGFFKDSII LATGATGTGK TLLVSKFIED
ACRNKERAIL FAYEESRAQL LRNGTSWGID FEQMEQDGLL KIICAYPEST GLEDHLQIIK
TDIGQFKPSR MAIDSLSALA RGVSHNAFRQ FVIGVTGYAK QEEIAGFFTN TSEEFMGSHS
ITDSHISTIT DTILMLQYVE IRGEMARALN VFKMRGSWHD KGIREFVITG NGPQIKDSFS
NFERIISGVP HRVTTDERSE LSRIARGVSS ED
