MUTS2_LISW6
ID MUTS2_LISW6 Reviewed; 785 AA.
AC A0AHX3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Endonuclease MutS2 {ECO:0000255|HAMAP-Rule:MF_00092};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00092};
GN Name=mutS2 {ECO:0000255|HAMAP-Rule:MF_00092}; OrderedLocusNames=lwe1187;
OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS NCTC 11857 / SLCC 5334 / V8).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=386043;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX PubMed=16936040; DOI=10.1128/jb.00758-06;
RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT genome reduction with Listeria innocua as compared to Listeria
RT monocytogenes.";
RL J. Bacteriol. 188:7405-7415(2006).
CC -!- FUNCTION: Endonuclease that is involved in the suppression of
CC homologous recombination and may therefore have a key role in the
CC control of bacterial genetic diversity. {ECO:0000255|HAMAP-
CC Rule:MF_00092}.
CC -!- SUBUNIT: Homodimer. {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}.
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DR EMBL; AM263198; CAK20605.1; -; Genomic_DNA.
DR RefSeq; WP_011702001.1; NC_008555.1.
DR AlphaFoldDB; A0AHX3; -.
DR SMR; A0AHX3; -.
DR STRING; 386043.lwe1187; -.
DR EnsemblBacteria; CAK20605; CAK20605; lwe1187.
DR GeneID; 61189070; -.
DR KEGG; lwe:lwe1187; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR Proteomes; UP000000779; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor 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 Gene3D; 3.30.1370.110; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00092; MutS2; 1.
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; IPR005747; MutS2.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002625; Smr_dom.
DR InterPro; IPR036063; Smr_dom_sf.
DR PANTHER; PTHR11361; PTHR11361; 1.
DR PANTHER; PTHR11361:SF14; PTHR11361:SF14; 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; SSF160443; SSF160443; 1.
DR SUPFAM; SSF48334; SSF48334; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01069; mutS2; 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.
FT CHAIN 1..785
FT /note="Endonuclease MutS2"
FT /id="PRO_1000075478"
FT DOMAIN 710..785
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT BINDING 335..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 785 AA; 86842 MW; FF00870663E65CB5 CRC64;
MEKKVEAILE FDKIKKQLTE FASSSLGEQA ILELAPATNF QVVQKSQLET EEGAKIIRLR
GSAPITGLTD VFAHLKRLEI GGDLNGLEIY QIGSNLRVSR QMKNFMTDLL EMGVELPLLG
ALSDELLVLK EVEEDIAISV DESGKILDTA SEALSTIRRT LRRTEDRVRE KLESYLRDRN
ASKMLSDAVI TIRNDRYVIP VKQEYKGHYG GIVHDQSASG QTLFIEPQSV VDLNNERKAL
QAKEKQEIER ILAEISASLA GWINEIHHNT FILGRYDFIF AKARFGKAMK AVTPHLSDAG
IVHLIAARHP LLDAANVVAN DIYLGEDFTT IVITGPNTGG KTITLKTLGL LTLMAQSGLQ
IPAQEDSTIA VFEHVFADIG DEQSIEQSLS TFSSHMTNIV SILEKVNHKS LILYDELGAG
TDPQEGAALA IAILDASHEK GASVVATTHY PELKAYGYNR VHATNASVEF NVETLSPTYK
LLIGVPGRSN AFDISRRLGL SENIITEARS LVDTESADLN DMISSLEEKR NLAETEYEEA
RELARGADAL LKDLQKEITN YYQQKDKLME QAREKAANIV TKAEVEAEEI IHELRTMQLN
GAAGIKEHEL IDAKTRLGKA KPKTINKTIP QAPKQKPHVF QVGDNVRVLS LGQKGTLLNK
ISDKEWNVQI GIIKMKIKTT DLEYIQPETP KKQRIITSVH SSDSPVKSEL DLRGERYEDA
LQKVDKYLDE ALLAGYPQVA IIHGKGTGAL RTGVTEYLKN HRMVKSIRFG AAAEGGNGVT
IVEFK