ID   MUTS2_LACCB             Reviewed;         786 AA.
AC   B3WC74;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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};
GN   OrderedLocusNames=LCABL_08520;
OS   Lacticaseibacillus casei (strain BL23) (Lactobacillus casei).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=543734;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL23;
RA   Maze A., Boel G., Bourand A., Loux V., Gibrat J.F., Zuniga M., Hartke A.,
RA   Deutscher J.;
RT   "Lactobacillus casei BL23 complete genome sequence.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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; FM177140; CAQ65975.1; -; Genomic_DNA.
DR   RefSeq; WP_012491200.1; NC_010999.1.
DR   AlphaFoldDB; B3WC74; -.
DR   SMR; B3WC74; -.
DR   KEGG; lcb:LCABL_08520; -.
DR   HOGENOM; CLU_011252_2_1_9; -.
DR   OMA; IHAIIND; -.
DR   OrthoDB; 256392at2; -.
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..786
FT                   /note="Endonuclease MutS2"
FT                   /id="PRO_1000093363"
FT   DOMAIN          711..786
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   REGION          682..709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         333..340
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ   SEQUENCE   786 AA;  86082 MW;  1E4B82B467015636 CRC64;
     MNEKILKTLE YDKIQQALLG QVVTANGRQL VQAMQPLTDP VAVQQALDET ADGASALRLK
     GGIPVPQLEN IDPALKRVDI GAVLNGQELA SISRVLQTVS AIDKFLTDLQ DQIDFRQLYT
     LQESLTVLPQ LSRRLKTAVD PDGTLTDEAS PQLHGVREQI KSIEGKIRGK MTNYTRGAQS
     KYLSDPIVTI RDDRYVIPVK AEYRAKFGGV VHDQSATGQT LFIEPQVIVA LNNRLREAQL
     AEVAEINRIL AELSNELAPY TGQIKANAAV LGHFDFINAK ARLAKAEKAT EPLVSADNDV
     LLRDARHPLI DPHKVVGNDI PLGDKYQAMV ITGPNTGGKT ITLKTLGLLQ LMGQSGLFIP
     ADDESRIGIF DEVFADIGDE QSIEQNLSTF SAHMDNIVHI LKQLSQNSLV LFDELGAGTD
     PQEGAALAIA ILDAVGEVGA YVVATTHYPE LKLYGYNTAK TINASMEFDS KTLQPTYRLL
     VGVPGRSNAF DISARLGLPS VIVERAKSMI SSDSHELNNM ISDLEKQRKA AETAYEAARR
     QLADAQSVHD ELAAAYKKFT TERDAQLQQA KDKANSLVDK AQTKADKIIK QLRQMQLTNP
     GTVKENQLIA AKTALKQLHQ DEPLQKNRIL RREREKQALH VGDEVKVASY DQTGTLLEQF
     DKKHWQVQLG ILKMKVPTDE MEKIKPSKQS AAQRPVVKVS GGGMSGPSTT LDLRGERYDQ
     AMADLDQYID AALLAGYPSV TIIHGLGTGA IRNGVTQYLK RNRQVKTYGF APQNAGGSGA
     TIVNFK