MUTS2_LACJO
ID MUTS2_LACJO Reviewed; 788 AA.
AC Q74KU8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=LJ_0479;
OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=257314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNCM I-1225 / La1 / NCC 533;
RX PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT johnsonii NCC 533.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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; AE017198; AAS08471.1; -; Genomic_DNA.
DR RefSeq; WP_011161611.1; NC_005362.1.
DR AlphaFoldDB; Q74KU8; -.
DR SMR; Q74KU8; -.
DR STRING; 257314.LJ_0479; -.
DR EnsemblBacteria; AAS08471; AAS08471; LJ_0479.
DR KEGG; ljo:LJ_0479; -.
DR PATRIC; fig|257314.6.peg.506; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR Proteomes; UP000000581; 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 CDD; cd03280; ABC_MutS2; 1.
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; PS50828; SMR; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..788
FT /note="Endonuclease MutS2"
FT /id="PRO_1000093366"
FT DOMAIN 713..788
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT BINDING 334..341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 788 AA; 88493 MW; 7AB4DA60769D36E3 CRC64;
MNSKIIEKLE YNRIIKQLSD LAITVPAKEQ ALTLMPSSNF DEVKKSIDQT RVLSNVLRVK
GPMPITDFKD VRASLKRLKV KANLNGEELG NIFLILSLAK DVSQFTADLE EREIDTRPIE
KTLKNLAIPE DLFKKLNQAI EYDGTVKDTA SSKLMQLRHD IQSNETDIKN HMNDYISGKH
TQYLSENIVT IRDGRYVLPV KQEYKNKFGG VVHDQSASGQ TLFVEPQAVL VLNNRQQNLM
AQERQEIHRI LIELSELAGM YQKEIKNNAD ALTQLDFLSA KSKLAKAMKA TEPVLNQDHV
IKLRKARHPL IDPKKVVPNN IELGTSFDTM LITGPNTGGK TITLKTLGLL QLMAQAGLFI
TAEEGSQLTV FNEIYADIGD EQSIEQSLST FSSHMDQIIK IMKDVTEDDL VLIDELGAGT
DPEEGASLAI AILDDLRGAQ AKIAITTHYP ELKLYGYNRA RTTNASMEFD LKKLAPTYRL
RIGIPGQSNA FAIAHQLGMN EVVVDKARSL MNDEDSDINK MIERLTEQTK AAEQLHETLK
QNVDQSITLK RQLQNGLDWY NQQVQKQLEK AQEKADEMLA KKRQKADKII NDLEEQRRAG
GQVRTNKVIE AKGALNKLER ENQNLAQNKV LQREKRRHDV SVGDTVKVLS YGQQGVITKK
LADHEFEVQI GILKVKVTDR DVEKISTQAA PKKAERAVRS SRDLRSTRAS SELDLRGQRY
EEALTNLDRY IDSSLLAGLN TVTIIHGIGT GAIRNGVQQY LKRNRHVKSY SYAPANQGGT
GATIVYLQ