Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Circadian clock protein KaiA

Gene

kaiA

Organism
Thermosynechococcus elongatus (strain BP-1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. In the complex, it enhances the phosphorylation status of KaiC. In contrast, the presence of KaiB in the complex decreases the phosphorylation status of KaiC, suggesting that KaiB acts by antagonizing the interaction between KaiA and KaiC. A KaiA dimer is sufficient to enhance KaiC hexamer phosphorylation.

GO - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

  • circadian rhythm Source: UniProtKB
  • protein phosphorylation Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Biological rhythms

Names & Taxonomyi

Protein namesi
Recommended name:
Circadian clock protein KaiA
Gene namesi
Name:kaiA
Ordered Locus Names:tlr0481
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
Proteomesi
  • UP000000440 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi204 – 2041Y → F: Induces a change in the structure diue to the absence of the hydrogen bond between D-266 and Y-204. 1 Publication
Mutagenesisi266 – 2661D → N: No effect. 1 Publication
Mutagenesisi270 – 2701H → A: Induces a decrease in activity and ability to enhance KaiC phosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 283283Circadian clock protein KaiAPRO_0000217869Add
BLAST

Interactioni

Subunit structurei

Homodimer. Component of the KaiABC complex, at least composed of a KaiC homohexamer, a KaiB dimer and two KaiA dimers. The KaiABC complex also interacts with SasA (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-701584,EBI-701584
kaiCQ79V6011EBI-701584,EBI-701595

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

DIPiDIP-29355N.
IntActiQ79V62. 1 interaction.
MINTiMINT-1954101.
STRINGi197221.tlr0481.

Structurei

Secondary structure

1
283
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi174 – 1818Combined sources
Helixi187 – 20317Combined sources
Helixi211 – 22515Combined sources
Helixi229 – 24618Combined sources
Helixi251 – 2599Combined sources
Helixi260 – 27617Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q6ANMR-A/B180-283[»]
1Q6BNMR-A/B180-283[»]
1SUYNMR-A/B180-283[»]
1SV1NMR-A/B180-283[»]
1V2ZX-ray1.80A174-283[»]
ProteinModelPortaliQ79V62.
SMRiQ79V62. Positions 174-278.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ79V62.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 163161KaiA N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini173 – 281109KaiA C-terminalPROSITE-ProRule annotationAdd
BLAST

Domaini

The KaiA domain mediates the interaction with KaiC, the homodimerization, and is responsible for the clock oscillation function.

Sequence similaritiesi

Contains 1 kaiA C-terminal domain.PROSITE-ProRule annotation
Contains 1 kaiA N-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108WXF. Bacteria.
ENOG410YS5X. LUCA.
HOGENOMiHOG000276784.
KOiK08480.
OMAiISSHIEQ.
OrthoDBiEOG65QWP2.

Family and domain databases

Gene3Di1.10.1240.30. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR011648. Circadian_clock_KaiA.
IPR020844. Circadian_clock_KaiA_N.
IPR020856. Circadian_clock_protein_KaiA_C.
IPR017944. KaiA/RbsU_helical_domain.
[Graphical view]
PfamiPF07688. KaiA. 1 hit.
[Graphical view]
SMARTiSM01247. KaiA. 1 hit.
[Graphical view]
SUPFAMiSSF101215. SSF101215. 1 hit.
SSF52172. SSF52172. 1 hit.
PROSITEiPS51431. KAIA_C. 1 hit.
PS51430. KAIA_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q79V62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQSTALTIC GLVYSPAIGQ ELVRLHTSDI DELVYFSSER EFCNYLEARR
60 70 80 90 100
NSIACLILEW GEGTPQIITY LHHSATLLPA ILIFPAAPAP PPAGPHYHIA
110 120 130 140 150
EVILTTDQLD QLNRQIEEAI TGFVKLCPGC AVPPHVLFRL PALKESSNVD
160 170 180 190 200
PQHRLSQKLK ERLGYLGVYY KRDTAFFFRR MSPADKRKLL DELRSIYRTI
210 220 230 240 250
VLEYFNTDAK VNERIDEFVS KAFFADISVS QVLEIHVELM DTFSKQLKLE
260 270 280
GRSEDILLDY RLTLIDVIAH LCEMYRRSIP REV
Length:283
Mass (Da):32,368
Last modified:July 5, 2004 - v1
Checksum:iD3B0DCBE8A580B4E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB071375 Genomic DNA. Translation: BAB85983.1.
BA000039 Genomic DNA. Translation: BAC08033.1.
RefSeqiNP_681271.1. NC_004113.1.
WP_011056332.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC08033; BAC08033; BAC08033.
GeneIDi1012550.
KEGGitel:tlr0481.
PATRICi23926206. VBITheElo119873_0506.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB071375 Genomic DNA. Translation: BAB85983.1.
BA000039 Genomic DNA. Translation: BAC08033.1.
RefSeqiNP_681271.1. NC_004113.1.
WP_011056332.1. NC_004113.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q6ANMR-A/B180-283[»]
1Q6BNMR-A/B180-283[»]
1SUYNMR-A/B180-283[»]
1SV1NMR-A/B180-283[»]
1V2ZX-ray1.80A174-283[»]
ProteinModelPortaliQ79V62.
SMRiQ79V62. Positions 174-278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29355N.
IntActiQ79V62. 1 interaction.
MINTiMINT-1954101.
STRINGi197221.tlr0481.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC08033; BAC08033; BAC08033.
GeneIDi1012550.
KEGGitel:tlr0481.
PATRICi23926206. VBITheElo119873_0506.

Phylogenomic databases

eggNOGiENOG4108WXF. Bacteria.
ENOG410YS5X. LUCA.
HOGENOMiHOG000276784.
KOiK08480.
OMAiISSHIEQ.
OrthoDBiEOG65QWP2.

Miscellaneous databases

EvolutionaryTraceiQ79V62.

Family and domain databases

Gene3Di1.10.1240.30. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR011648. Circadian_clock_KaiA.
IPR020844. Circadian_clock_KaiA_N.
IPR020856. Circadian_clock_protein_KaiA_C.
IPR017944. KaiA/RbsU_helical_domain.
[Graphical view]
PfamiPF07688. KaiA. 1 hit.
[Graphical view]
SMARTiSM01247. KaiA. 1 hit.
[Graphical view]
SUPFAMiSSF101215. SSF101215. 1 hit.
SSF52172. SSF52172. 1 hit.
PROSITEiPS51431. KAIA_C. 1 hit.
PS51430. KAIA_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Crystal structure of the C-terminal clock-oscillator domain of the cyanobacterial KaiA protein."
    Uzumaki T., Fujita M., Nakatsu T., Hayashi F., Shibata H., Itoh N., Kato H., Ishiura M.
    Nat. Struct. Mol. Biol. 11:623-631(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 174-278, MUTAGENESIS OF TYR-204; ASP-266 AND HIS-270.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BP-1.
  3. "NMR structure of the KaiC-interacting C-terminal domain of KaiA, a circadian clock protein: implications for KaiA-KaiC interaction."
    Vakonakis I., Sun J., Wu T., Holzenburg A., Golden S.S., LiWang A.C.
    Proc. Natl. Acad. Sci. U.S.A. 101:1479-1484(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 180-283.
  4. "Structure of the C-terminal domain of the clock protein KaiA in complex with a KaiC-derived peptide: implications for KaiC regulation."
    Vakonakis I., LiWang A.C.
    Proc. Natl. Acad. Sci. U.S.A. 101:10925-10930(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 180-283 IN COMPLEX WITH 488-518 OF KAIC.

Entry informationi

Entry nameiKAIA_THEEB
AccessioniPrimary (citable) accession number: Q79V62
Secondary accession number(s): Q8RR35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.