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UniProt functional annotation for Q5SI82 | ||
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| UniProt code: Q5SI82. |
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| Organism: | |
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). |
| Taxonomy: | |
Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus. |
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| Function: | |
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. {ECO:0000255|HAMAP- Rule:MF_01458}. |
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| Function: | |
Degrades preferentially unfolded substrates in a processive, ATP-dependent manner, usually after hydrophobic residues. |
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| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01458}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01458}; |
| Activity regulation: | |
The proteolytic activity is dependent on ATP, both the ATPase and protease activities are inhibited by ADP. {ECO:0000269|PubMed:10788805}. |
| Subunit: | |
The isolated soluble domain (residues 126-624) forms a stable hexamer in which the AAA+ domains (residues 126-400) are alternatively open or closed. {ECO:0000269|PubMed:16762831}. |
| Subcellular location: | |
Cell inner membrane {ECO:0000305|PubMed:10788805}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01458}; Cytoplasmic side {ECO:0000255|HAMAP- Rule:MF_01458}. |
| Domain: | |
The open AAA+ domain (residues 126-400) probably allows nucleotide exchange and has the protease active site, while the closed domain is the active ATPase domain but the protease is inactive. |
| Similarity: | |
In the central section; belongs to the AAA ATPase family. {ECO:0000255|HAMAP-Rule:MF_01458}. |
| Similarity: | |
In the C-terminal section; belongs to the peptidase M41 family. {ECO:0000255|HAMAP-Rule:MF_01458}. |
Annotations taken from UniProtKB at the EBI.