KAIA_NOSS1
ID KAIA_NOSS1 Reviewed; 102 AA.
AC Q8YT42;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Circadian clock protein KaiA;
GN Name=kaiA; OrderedLocusNames=alr2884;
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), HOMODIMERIZATION, AND MUTAGENESIS OF
RP ARG-69.
RX PubMed=15071498; DOI=10.1038/sj.emboj.7600190;
RA Garces R.G., Wu N., Gillon W., Pai E.F.;
RT "Anabaena circadian clock proteins KaiA and KaiB reveal a potential common
RT binding site to their partner KaiC.";
RL EMBO J. 23:1688-1698(2004).
CC -!- FUNCTION: Component of the KaiABC clock protein complex, which
CC constitutes the main circadian regulator in cyanobacteria. The KaiABC
CC complex may act as a promoter-nonspecific transcription regulator that
CC represses transcription, possibly by acting on the state of chromosome
CC compaction. In the complex, it enhances the phosphorylation status of
CC KaiC. In contrast, the presence of KaiB in the complex decreases the
CC phosphorylation status of KaiC, suggesting that KaiB acts by
CC antagonizing the interaction between KaiA and KaiC. A KaiA dimer is
CC sufficient to enhance KaiC hexamer phosphorylation (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Component of the KaiABC complex, at least composed
CC of a KaiC homohexamer, a KaiB dimer and two KaiA dimers. The KaiABC
CC complex also interacts with SasA (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The KaiA domain mediates the interaction with KaiC, the
CC homodimerization, and is responsible for the clock oscillation
CC function. {ECO:0000250}.
CC -!- MISCELLANEOUS: Lacks an N-terminus part downstream the KaiA domain,
CC which may be involved in transducing input signals to the KaiABC
CC complex.
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DR EMBL; AB071284; BAB85867.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB74583.1; -; Genomic_DNA.
DR PIR; AE2166; AE2166.
DR RefSeq; WP_010997035.1; NZ_RSCN01000003.1.
DR PDB; 1R5Q; X-ray; 2.00 A; A=1-102.
DR PDBsum; 1R5Q; -.
DR AlphaFoldDB; Q8YT42; -.
DR SMR; Q8YT42; -.
DR STRING; 103690.17131978; -.
DR EnsemblBacteria; BAB74583; BAB74583; BAB74583.
DR KEGG; ana:alr2884; -.
DR eggNOG; ENOG502Z8HQ; Bacteria.
DR OMA; LCEAYRG; -.
DR OrthoDB; 1644154at2; -.
DR EvolutionaryTrace; Q8YT42; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0007623; P:circadian rhythm; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.10.1240.30; -; 1.
DR InterPro; IPR011648; Circadian_clock_KaiA.
DR InterPro; IPR020856; Circadian_clock_protein_KaiA_C.
DR InterPro; IPR017944; KaiA/RbsU_helical_domain_sf.
DR Pfam; PF07688; KaiA; 1.
DR SMART; SM01247; KaiA; 1.
DR SUPFAM; SSF101215; SSF101215; 1.
DR PROSITE; PS51431; KAIA_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biological rhythms; Reference proteome.
FT CHAIN 1..102
FT /note="Circadian clock protein KaiA"
FT /id="PRO_0000217868"
FT DOMAIN 1..102
FT /note="KaiA C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00761"
FT MUTAGEN 69
FT /note="R->A: Abolishes the interaction with KaiC."
FT /evidence="ECO:0000269|PubMed:15071498"
FT HELIX 8..24
FT /evidence="ECO:0007829|PDB:1R5Q"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:1R5Q"
FT HELIX 50..67
FT /evidence="ECO:0007829|PDB:1R5Q"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1R5Q"
FT HELIX 82..100
FT /evidence="ECO:0007829|PDB:1R5Q"
SQ SEQUENCE 102 AA; 11965 MW; 552AA7370BA9D74C CRC64;
MTQEVDQQIL LQQLKSDYRQ ILLSYFTTDK ALKEKIDKFI NAVFCANIPV PEIIEIHMEL
IDEFSKQLRL EGRGDETLMD YRLTLIDILA HLCEAYRGAI FK