ID B7C7S5_9FIRM Unreviewed; 774 AA.
AC B7C7S5;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Endonuclease MutS2 {ECO:0000256|HAMAP-Rule:MF_00092};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00092};
GN Name=mutS2 {ECO:0000256|HAMAP-Rule:MF_00092};
GN ORFNames=EUBIFOR_00225 {ECO:0000313|EMBL:EEC91181.1};
OS Holdemanella biformis DSM 3989.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Holdemanella.
OX NCBI_TaxID=518637 {ECO:0000313|EMBL:EEC91181.1, ECO:0000313|Proteomes:UP000004315};
RN [1] {ECO:0000313|EMBL:EEC91181.1, ECO:0000313|Proteomes:UP000004315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC91181.1,
RC ECO:0000313|Proteomes:UP000004315};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEC91181.1, ECO:0000313|Proteomes:UP000004315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC91181.1,
RC ECO:0000313|Proteomes:UP000004315};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium biforme (DSM 3989).";
RL Submitted (NOV-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:0000256|HAMAP-
CC Rule:MF_00092}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00092}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00092}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEC91181.1}.
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DR EMBL; ABYT01000020; EEC91181.1; -; Genomic_DNA.
DR AlphaFoldDB; B7C7S5; -.
DR STRING; 518637.EUBIFOR_00225; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OrthoDB; 9808166at2; -.
DR Proteomes; UP000004315; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis 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; P-loop containing nucleotide triphosphate hydrolases; 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; IPR046893; MSSS.
DR InterPro; IPR005747; MutS2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002625; Smr_dom.
DR InterPro; IPR036063; Smr_dom_sf.
DR PANTHER; PTHR48378:SF1; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48378; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF20297; MSSS; 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; SSF48334; DNA repair protein MutS, domain III; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF160443; SMR domain-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50828; SMR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00092}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00092};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00092}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00092};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00092};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00092}.
FT DOMAIN 699..774
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT COILED 502..598
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 337..344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ SEQUENCE 774 AA; 87054 MW; CF2357FCFFEE18D7 CRC64;
MECFMKRNFR DELNQAIDFS SVLTQICAFS SFSCSKEKIL NALPQFNKLE IQEQLNYAKE
AIQFEQKGGL LNLSGANDIS LPVSKAEKQM PLTSKELISI YHFLTAVKQA KQSLNSSEFI
ELTNLAQSMD GCTRLMDSII SKIDLTGSVK EDATPALKSM HKALVDTRLA LQSKSRQFLK
KNSSKLMENM TTTVSGRVVV LVRAQDKNAF GGMIHGQSSS GLAYYVEPSS FVADNNEISS
LVIRIEEEKK RICKELSMQV KKHALALTSA LETLTIIDVA FTKAKWAIRY DGCIPSLQSR
DHSLYLEHAK HPLIDEKKVV CNTYELNDQQ ACLMISGPNM GGKTVTLKTI GLFVALAHAA
FPVLCHKAIL PFYQSMYFDI GDHQSIENNL STFSSHISRL SHICQKSDEN SFILLDEIGN
GTDPLEGASL AVAILEYLIS KKSTIITSTH YSQVKTYGKA NEHVLVSSVE FDPETLKPTY
KYIPGVSGAS YAFHIAREYH LEESILKRAD FLKNENEKQT EKELEKLEKL QNDVLKQKER
FNALIEDAHR VQKEAYEKEK EIEKRKAELD ASYQEQLNEM LEKKKAQAKE ILTVLRKQKT
GKQHEQIEKM HELDLLSENV VEEEQEKKEF KVGDYVKISG LNSHGEIVDI RRNEATVLTN
GMKMKVKLSK LEPMHKPQIK KTTYKAHVES VSSRFPLELN LIGMRVEEGI AALDKYLDQA
VVKHIKQVRI IHGMGTGALR TAVWKDLKKQ PNVSKFTSAG PSEGGLGATI VILK
//
