HAMAP rule MF_01837
General rule information
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| Accession | MF_01837 |
| Dates | 13-SEP-2004 (Created)
17-FEB-2023 (Last updated, Version 18) |
| Name | Kinase_SasA |
| Scope(s) |
Bacteria Cyanobacteriota |
| Template(s) | Q06904 (SASA_SYNE7); [ Recover all ] |
| Triggered by |
HAMAP; MF_01837 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | SASA |
| Protein name | RecName: Full=Adaptive-response sensory-kinase SasA; EC=2.7.13.3; AltName: Full=Sensor histidine kinase SasA; |
| Gene name | Name=sasA; |
Comments
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| FUNCTION | Member of the two-component regulatory system SasA/RpaA involved in genome-wide circadian gene expression. One of several clock output pathways. Participates in the Kai clock protein complex, the main circadian regulator in cyanobacteria, via its interaction with KaiC. KaiC enhances the autophosphorylation activity of SasA, which then transfers its phosphate group to RpaA to activate it. In addition to its output function, recruits fold-shifted KaiB (KaiB(fs)) to KaiC to cooperatively form the KaiB(6):KaiC(6) complex (independent of SasA kinase activity). Required for robustness of the circadian rhythm of gene expression and is involved in clock output, also required for adaptation to light/dark cycles. |
| CATALYTIC ACTIVITY | Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L- histidine.; EC=2.7.13.3; |
| case not <OC:Prochlorococcus> | |
| SUBUNIT | Homooligomerizes. Interacts with KaiC. Participates in the KaiABC clock complex, whose core is composed of a KaiC homohexamer, 6 KaiB and up to 6 KaiA dimers. SasA and KaiB(fs) compete to bind to KaiC. |
| end case | |
| case <OC:Prochlorococcus> | |
| SUBUNIT | Homooligomerizes. Interacts with KaiC. Participates in the KaiBC complex, whose core is composed of a KaiC homohexamer and 6 KaiB. |
| end case | |
| DOMAIN | The N-terminus interacts with KaiC, while the C-terminal histidine kinase domain autophosphorylates and is probably responsible for self-oligomerization. The N-terminal domain stimulates the C- terminus to autophosphorylate. |
Keywords
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| ATP-binding |
| Nucleotide-binding |
| Biological rhythms |
| Kinase |
| Phosphoprotein |
| Transferase |
| Two-component regulatory system |
Gene Ontology
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| GO:0007623; Biological process:circadian rhythm |
| GO:0004673; Molecular function:protein histidine kinase activity |
Cross-references
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| Pfam | PF02518; HATPase_c; 1; |
| Pfam | PF00512; HisKA; 1; |
| Pfam | PF07689; KaiB; 1; |
| PRINTS | PR00344; BCTRLSENSOR; 1; |
| PROSITE | PS50109; HIS_KIN; 1; |
Features
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| From: SASA_SYNE7 (Q06904) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| MOD_RES | 161 | 161 | /note="Phosphohistidine; by autocatalysis" | H | ||||||||
Additional information
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| Size range | 370-401 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |