MUTS2_LACLS
ID MUTS2_LACLS Reviewed; 776 AA.
AC Q02XM1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=LACR_1809;
OS Lactococcus lactis subsp. cremoris (strain SK11).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=272622;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK11;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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; CP000425; ABJ73301.1; -; Genomic_DNA.
DR RefSeq; WP_011676549.1; NC_008527.1.
DR AlphaFoldDB; Q02XM1; -.
DR SMR; Q02XM1; -.
DR EnsemblBacteria; ABJ73301; ABJ73301; LACR_1809.
DR KEGG; llc:LACR_1809; -.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR Proteomes; UP000000240; 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; 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..776
FT /note="Endonuclease MutS2"
FT /id="PRO_1000093369"
FT DOMAIN 701..776
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT BINDING 330..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 776 AA; 87288 MW; 5E1E5AD10D27DC08 CRC64;
MNKKILQILE YDKVKEQFMN ALTTAQGQKE LSDLVPLTDK DKIQLLFDEV ADFRLLTQEN
GLLNLGKTND LTEILRRLEL EASLSGKEFV EIKKVIQLGI NIQRFFDEAE NVETPSLNIT
LEKLVDLSGL IKKLEIFDNA GSLYDNASLE LMHIRSSIKS HQSEIRKIMQ EMLTKNLASL
SENVITIRND RQVLPVKAEN KNKIAGVVHD MSASGQTLYI EPNAVVSLNN KLNQKRIEER
QEITRIYREL AEELKPYSFD IRQNAWLIGH IDFVRAKYLY LAANKASLPA LTNDKDIILF
AARHPLIDAK MVVANDIKFD RTLNTIVITG PNTGGKTITL KTVGLLTILA QSGLPILADD
GSRIHLFDDI FADIGDEQSI EQSLSTFSSH MTNIVQILAQ ADENSLVLFD ELGAGTDPKE
GAALAIAILE NLRKRNVKTM ASTHYPELKA YGVKTQQVIN ASMEFNIDKM QPTYHLQLGV
PGRSNALEIS RRLGLPETII SEAGQQISGS EHDVNQMIEK LEEKTREVIE SSRNIKKIER
ENQSLHKDLT KVYNQINRER DFELEKAQKE AQEVVKKASL EAQEILKNLN DKAALKPHEI
IAARKELEGL APTIDFSKNK VLKKAKAQRG LKQGAEVNVT SYGQRGKLIR LEKDGRWTVQ
MGSITTRLSE EEFEVIETPE QIQAKTKNVS KKVTSKVKAQ LDLRGMRYEE AELELDNYID
QALLANLIQI TIVHGIGTGV IREMVQKKLQ KHRHIKSYEY APINAGGSGA TIAILK