AC MF_00092; DC Protein; auto TR HAMAP; MF_00092; -; 1; level=0 XX Names: MutS2 XX ID MUTS2 DE RecName: Full=Endonuclease MutS2; DE EC=3.1.-.-; DE AltName: Full=Ribosome-associated protein quality control-upstream factor; DE Short=RQC-upstream factor; DE Short=RqcU; DE EC=3.6.4.-; GN Name=mutS2; Synonyms=rqcU; XX CC -!- FUNCTION: Endonuclease that is involved in the suppression of CC homologous recombination and thus may have a key role in the control of CC bacterial genetic diversity. CC -!- FUNCTION: Acts as a ribosome collision sensor, splitting the ribosome CC into its 2 subunits. Detects stalled/collided 70S ribosomes which it CC binds and splits by an ATP-hydrolysis driven conformational change. CC Acts upstream of the ribosome quality control system (RQC), a ribosome- CC associated complex that mediates the extraction of incompletely CC synthesized nascent chains from stalled ribosomes and their subsequent CC degradation. Probably generates substrates for RQC. CC -!- SUBUNIT: Homodimer. Binds to stalled ribosomes, contacting rRNA. CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2 CC subfamily. XX DR Pfam; PF00488; MutS_V; 1; trigger=no DR Pfam; PF01713; Smr; 1; trigger=no DR PIRSF; PIRSF005814; MutS_YshD; 1; trigger=no DR NCBIfam; TIGR01069; MutS2; 1; trigger=no DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1; trigger=no DR PROSITE; PS50828; SMR; 1; trigger=yes XX KW ATP-binding KW DNA-binding KW Endonuclease KW Hydrolase KW Nuclease KW Nucleotide-binding KW RNA-binding KW rRNA-binding XX GO GO:0005524; F:ATP binding GO GO:0003677; F:DNA binding GO GO:0004519; F:endonuclease activity GO GO:0072344; P:rescue of stalled ribosome GO GO:0019843; F:rRNA binding GO GO:0043023; F:ribosomal large subunit binding XX FT From: MUTS2_THET8 (Q5SHT5) FT BINDING 315..322 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G-x-N-x-G-G-K-[TS] XX Size: 660-920; Related: None; Template: Q5SHT5; O25338; Q9X105; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: Endonuclease activity has been proven for T.thermophilus (Q5SHT5), T. maritima (Q9X105), D.radiodurans (Q9RSZ3) but could not be demonstrated in B. subtilis (P94545). XX # Version: 21 # Last updated date: 2024-09-02 # Created date: 2005-02-28 //