ID MUTS2_LACPL Reviewed; 787 AA. AC Q88V16; F9UQJ0; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-NOV-2024, entry version 120. DE RecName: Full=Endonuclease MutS2 {ECO:0000255|HAMAP-Rule:MF_00092}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00092}; DE AltName: Full=Ribosome-associated protein quality control-upstream factor {ECO:0000255|HAMAP-Rule:MF_00092}; DE Short=RQC-upstream factor {ECO:0000255|HAMAP-Rule:MF_00092}; DE Short=RqcU {ECO:0000255|HAMAP-Rule:MF_00092}; DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_00092}; GN Name=mutS2 {ECO:0000255|HAMAP-Rule:MF_00092}; GN Synonyms=rqcU {ECO:0000255|HAMAP-Rule:MF_00092}; OrderedLocusNames=lp_2271; OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) OS (Lactobacillus plantarum). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactiplantibacillus. OX NCBI_TaxID=220668; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX PubMed=12566566; DOI=10.1073/pnas.0337704100; RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., RA Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; RX PubMed=22156394; DOI=10.1128/jb.06275-11; RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M., RA Kleerebezem M., van Hijum S.A.; RT "Complete resequencing and reannotation of the Lactobacillus plantarum RT WCFS1 genome."; RL J. Bacteriol. 194:195-196(2012). 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. {ECO:0000255|HAMAP-Rule:MF_00092}. 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. {ECO:0000255|HAMAP- CC Rule:MF_00092}. CC -!- SUBUNIT: Homodimer. Binds to stalled ribosomes, contacting rRNA. CC {ECO:0000255|HAMAP-Rule:MF_00092}. CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00092}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL935263; CCC79479.1; -; Genomic_DNA. DR RefSeq; WP_011101700.1; NC_004567.2. DR RefSeq; YP_004889993.1; NC_004567.2. DR AlphaFoldDB; Q88V16; -. DR SMR; Q88V16; -. DR STRING; 220668.lp_2271; -. DR DNASU; 1061270; -. DR EnsemblBacteria; CCC79479; CCC79479; lp_2271. DR KEGG; lpl:lp_2271; -. DR PATRIC; fig|220668.9.peg.1922; -. DR eggNOG; COG1193; Bacteria. DR HOGENOM; CLU_011252_2_1_9; -. DR OrthoDB; 9808166at2; -. DR PhylomeDB; Q88V16; -. DR Proteomes; UP000000432; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro. DR GO; GO:0006298; P:mismatch repair; IEA:InterPro. DR GO; GO:0045910; P:negative regulation of DNA recombination; IEA:InterPro. DR FunFam; 3.40.50.300:FF:000830; Endonuclease MutS2; 1. DR Gene3D; 1.10.1420.10; -; 2. DR Gene3D; 3.30.1370.110; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00092; MutS2; 1. DR InterPro; IPR050184; Bact_DNA_MMR_MutS2. DR InterPro; IPR000432; DNA_mismatch_repair_MutS_C. DR InterPro; IPR007696; DNA_mismatch_repair_MutS_core. DR InterPro; IPR036187; DNA_mismatch_repair_MutS_sf. DR InterPro; IPR046893; MSSS. DR InterPro; IPR005747; MutS2. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR002625; Smr_dom. DR InterPro; IPR036063; Smr_dom_sf. DR NCBIfam; TIGR01069; mutS2; 1. DR PANTHER; PTHR48378:SF1; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR48378; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR Pfam; PF20297; MSSS; 1. DR Pfam; PF00488; MutS_V; 1. DR Pfam; PF01713; Smr; 1. DR PIRSF; PIRSF005814; MutS_YshD; 1. DR SMART; SM00534; MUTSac; 1. DR SMART; SM00533; MUTSd; 1. DR SMART; SM00463; SMR; 1. DR SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF160443; SMR domain-like; 1. DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1. DR PROSITE; PS50828; SMR; 1. PE 3: Inferred from homology; KW ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease; KW Nucleotide-binding; Reference proteome; RNA-binding; rRNA-binding. FT CHAIN 1..787 FT /note="Endonuclease MutS2" FT /id="PRO_1000093370" FT DOMAIN 712..787 FT /note="Smr" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092" FT BINDING 336..343 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092" SQ SEQUENCE 787 AA; 87220 MW; F059F850A3E7BC39 CRC64; MNSKVLNTLE YQQVKQQLAP YLVSATGQQA LNELHPMTSV ADIQRALDET NDGAEVYRLK GGIPVARLAD IKPHMKRLAI GATLNGSELG QVGRVLRTTR AITRFFAELL EDAPENDIRH LFDEVAELVT LPDVTKRLAT AIEGDGHITD EASPELSRIR SNIRRTETEI RNQMGHYTRG HDAKYLSDPI ITIRNDRYVI PVKAENRSRF GGIVHDQSAS GQTLFIEPQA VMAMNDRLRQ NQVAEKQEEQ RILEELSNLI APYQDEIINN AAILGHFDFI NAKARYAHDM KATEPAVSPQ NEVYLRQARH PLIDPRKVVA NDISLGTDYQ AMVITGPNTG GKTITLKTLG LLQLMAQSGL FIPVEAGSRV GVYNEIFADI GDEQSIEQNL STFSSHMENI ESFLAQIDAH SLVLVDELGA GTDPQEGAAL AIAILDAIGA KGTQVVATTH YPELKAYGFN RPDTINASME FDEETLKPTY RLLVGIPGRS NALDIAQRLG IPQAIVDQAR SLTDTDSQDL NAMIADLVTK RKQVEDEQLH LKTQVADSEK LHRQLKSEFN AYQQRKDQLI EDAKVQANTI VEQSKTKADA IISDLRKKQL ASGTATVKEN ELIDAKGALN ALEQQPKLKK NRVLRRAKAQ HDFHEGDDVL VKSYGQRGVL MRQMGKHEWE VQLGILKMKI SDGDLERVKP EEPKRARATV QSAHASHVSP NLDLRGVRYE DAMTQVDRYI DAALLAGYPS VTIVHGKGTG ALREGITNYL KSNRQVKSFH FAAPNHGGNG ATEVQFK //