KAIA_THEVB
ID KAIA_THEVB Reviewed; 283 AA.
AC Q79V62; Q8RR35;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Circadian clock protein KaiA;
GN Name=kaiA; OrderedLocusNames=tlr0481;
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], X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF
RP 174-278, AND MUTAGENESIS OF TYR-204; ASP-266 AND HIS-270.
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=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 180-283.
RX PubMed=14749515; DOI=10.1073/pnas.0305516101;
RA Vakonakis I., Sun J., Wu T., Holzenburg A., Golden S.S., LiWang A.C.;
RT "NMR structure of the KaiC-interacting C-terminal domain of KaiA, a
RT circadian clock protein: implications for KaiA-KaiC interaction.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1479-1484(2004).
RN [4]
RP STRUCTURE BY NMR OF 180-283 IN COMPLEX WITH 488-518 OF KAIC.
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: 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.
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 -!- INTERACTION:
CC Q79V62; Q79V62: kaiA; NbExp=4; IntAct=EBI-701584, EBI-701584;
CC Q79V62; Q79V60: kaiC; NbExp=12; IntAct=EBI-701584, EBI-701595;
CC -!- DOMAIN: The KaiA domain mediates the interaction with KaiC, the
CC homodimerization, and is responsible for the clock oscillation
CC function.
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DR EMBL; AB071375; BAB85983.1; -; Genomic_DNA.
DR EMBL; BA000039; BAC08033.1; -; Genomic_DNA.
DR RefSeq; NP_681271.1; NC_004113.1.
DR RefSeq; WP_011056332.1; NC_004113.1.
DR PDB; 1Q6A; NMR; -; A/B=180-283.
DR PDB; 1Q6B; NMR; -; A/B=180-283.
DR PDB; 1SUY; NMR; -; A/B=180-283.
DR PDB; 1SV1; NMR; -; A/B=180-283.
DR PDB; 1V2Z; X-ray; 1.80 A; A=174-283.
DR PDB; 5JWR; X-ray; 2.61 A; E/F/G/H=147-283.
DR PDBsum; 1Q6A; -.
DR PDBsum; 1Q6B; -.
DR PDBsum; 1SUY; -.
DR PDBsum; 1SV1; -.
DR PDBsum; 1V2Z; -.
DR PDBsum; 5JWR; -.
DR AlphaFoldDB; Q79V62; -.
DR BMRB; Q79V62; -.
DR SMR; Q79V62; -.
DR DIP; DIP-29355N; -.
DR IntAct; Q79V62; 1.
DR MINT; Q79V62; -.
DR STRING; 197221.22294202; -.
DR EnsemblBacteria; BAC08033; BAC08033; BAC08033.
DR KEGG; tel:tlr0481; -.
DR PATRIC; fig|197221.4.peg.506; -.
DR eggNOG; ENOG502Z8HQ; Bacteria.
DR OMA; VMAHLCE; -.
DR OrthoDB; 1326064at2; -.
DR EvolutionaryTrace; Q79V62; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007623; P:circadian rhythm; TAS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.10.1240.30; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR011648; Circadian_clock_KaiA.
DR InterPro; IPR020844; Circadian_clock_KaiA_N.
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 SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51431; KAIA_C; 1.
DR PROSITE; PS51430; KAIA_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biological rhythms; Reference proteome.
FT CHAIN 1..283
FT /note="Circadian clock protein KaiA"
FT /id="PRO_0000217869"
FT DOMAIN 3..163
FT /note="KaiA N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00760"
FT DOMAIN 173..281
FT /note="KaiA C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00761"
FT MUTAGEN 204
FT /note="Y->F: Induces a change in the structure diue to the
FT absence of the hydrogen bond between D-266 and Y-204."
FT /evidence="ECO:0000269|PubMed:15170179"
FT MUTAGEN 266
FT /note="D->N: No effect."
FT /evidence="ECO:0000269|PubMed:15170179"
FT MUTAGEN 270
FT /note="H->A: Induces a decrease in activity and ability to
FT enhance KaiC phosphorylation."
FT /evidence="ECO:0000269|PubMed:15170179"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:5JWR"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:5JWR"
FT HELIX 174..181
FT /evidence="ECO:0007829|PDB:1V2Z"
FT HELIX 187..203
FT /evidence="ECO:0007829|PDB:1V2Z"
FT HELIX 211..225
FT /evidence="ECO:0007829|PDB:1V2Z"
FT HELIX 229..246
FT /evidence="ECO:0007829|PDB:1V2Z"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:1V2Z"
FT HELIX 260..276
FT /evidence="ECO:0007829|PDB:1V2Z"
SQ SEQUENCE 283 AA; 32368 MW; D3B0DCBE8A580B4E CRC64;
MAQSTALTIC GLVYSPAIGQ ELVRLHTSDI DELVYFSSER EFCNYLEARR NSIACLILEW
GEGTPQIITY LHHSATLLPA ILIFPAAPAP PPAGPHYHIA EVILTTDQLD QLNRQIEEAI
TGFVKLCPGC AVPPHVLFRL PALKESSNVD PQHRLSQKLK ERLGYLGVYY KRDTAFFFRR
MSPADKRKLL DELRSIYRTI VLEYFNTDAK VNERIDEFVS KAFFADISVS QVLEIHVELM
DTFSKQLKLE GRSEDILLDY RLTLIDVIAH LCEMYRRSIP REV
