MUTS2_LACE2
ID MUTS2_LACE2 Reviewed; 787 AA.
AC C4Z417;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=EUBELI_01853;
OS Lachnospira eligens (strain ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4)
OS (Eubacterium eligens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnospira.
OX NCBI_TaxID=515620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4;
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; CP001104; ACR72842.1; -; Genomic_DNA.
DR RefSeq; WP_012740074.1; NC_012778.1.
DR AlphaFoldDB; C4Z417; -.
DR SMR; C4Z417; -.
DR STRING; 515620.EUBELI_01853; -.
DR PRIDE; C4Z417; -.
DR EnsemblBacteria; ACR72842; ACR72842; EUBELI_01853.
DR GeneID; 41356503; -.
DR KEGG; eel:EUBELI_01853; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OMA; IHAIIND; -.
DR OrthoDB; 256392at2; -.
DR Proteomes; UP000001476; 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..787
FT /note="Endonuclease MutS2"
FT /id="PRO_1000202679"
FT DOMAIN 712..787
FT /note="Smr"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT BINDING 329..336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
SQ SEQUENCE 787 AA; 86628 MW; D63D9E9A1CAEF713 CRC64;
MNKKSLSTLE FYKITDQLVS YACCDGAKKI LRNLKPMTDI TDINLRLNET NDALSRIFQK
GTVDFSQTKD IRASVARLKV GSSLNISELL NISAILSCAK HVKDYYEHRE DSISGMLENL
ATVDALNSQI KKCIISEDEI SDDASSNLRS IRRSKSIAND RIHSELNKLL NSPTYRTYLQ
DYVITTRQGR YCLPVKAEYK SAFPGMIHDQ SSTGSTLFIE PAAVVKLNND IRELELKEAA
EIEVILADLS AKAGEHTEEL LCDYEILVEL DCIFAKAQLA RHMHASRPVM NTSGIINIKK
GRHPLIESHT VVPIDIYLGT DFKLLIITGP NTGGKTVSLK TVGLLTLMAQ SGLFIPALDH
SDIAVFKNIY ADIGDEQSIE QSLSTFSSHM TNTVKILKEA DENCLVLFDE IGAGTDPTEG
AALAIAILND LKMRGVTTMA TTHYSEIKLY ALSTEGVENA SCEFDVESLR PTYRLLIGIP
GKSNAFAISK KLGLPDYILS DASERLNAED VHFEDIVSDL EHARISLEKE QAEVESYKAE
IASLKEKLQA KNERLDERTD NIIRKANEQA AAILKDAKDF ADETIKAMNK HGMTVAELEK
HRTAVREKMN KNQAKLKVEP AKVKAHKAHD ISEFKTGMHV KVLTMNVSGT VSAIHPAKKQ
VTVQVGALST KIDIKNLEIL SDYKEPKEAP SKAAGGSGKI KMSKSAGIST EINLLGCTVD
EAVARLDKYL DDAYIARIPQ VRIVHGKGTG ALRNGVTAYL RGVPYIKSFR LGEIGEGDAG
VTIVDFK