|
|
||
|
|
|
|
|
UniProt functional annotation for Q5SHT5 | ||
|
|
|
|
|
|
||
| UniProt code: Q5SHT5. |
|
||
| Organism: | |
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). |
| Taxonomy: | |
Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus. |
|
||
|
||
| Function: | |
Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity. Cleaves the phosphate backbone of oligodeoxynucleotides non-sequence-specifically at the 3' side of the phosphates. Preferably incises the branched DNA structures, especially the D-loop structure over the Holliday junction. Has ATPase activity. Binds to dsDNA but not to ssDNA. {ECO:0000255|HAMAP- Rule:MF_00092, ECO:0000269|PubMed:15113836, ECO:0000269|PubMed:17215294, ECO:0000269|PubMed:17686785, ECO:0000269|PubMed:18838375}. |
|
||
| Activity regulation: | |
Nuclease activity is stimulated by interaction with MutL. ATPase activity is stimulated by dsDNA. {ECO:0000269|PubMed:15113836}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=48 uM for ATP {ECO:0000269|PubMed:17215294}; Note=kcat is 2.1 min(-1) for ATP.; |
| Subunit: | |
Homodimer. Interacts with MutL. {ECO:0000255|HAMAP- Rule:MF_00092, ECO:0000269|PubMed:15113836, ECO:0000269|PubMed:17215294}. |
| Domain: | |
Contains an N-terminal DNA-binding domain, followed by a dimerization domain and a C-terminal domain, called the small MutS- related (Smr) domain, which is absent from MutS and contains the endonuclease activity. The Smr domain can also bind DNA. {ECO:0000269|PubMed:17215294}. |
| Disruption phenotype: | |
Disruption causes an increase in the frequency of recombination between perfectly matched sequences. {ECO:0000269|PubMed:18838375}. |
| Similarity: | |
Belongs to the DNA mismatch repair MutS family. MutS2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00092}. |
Annotations taken from UniProtKB at the EBI.