ID A0A151AU23_9CLOT Unreviewed; 788 AA.
AC A0A151AU23;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 ECO:0000313|EMBL:KYH31060.1};
GN ORFNames=CLTEP_24370 {ECO:0000313|EMBL:KYH31060.1};
OS Clostridium tepidiprofundi DSM 19306.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121338 {ECO:0000313|EMBL:KYH31060.1, ECO:0000313|Proteomes:UP000075531};
RN [1] {ECO:0000313|EMBL:KYH31060.1, ECO:0000313|Proteomes:UP000075531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19306 {ECO:0000313|EMBL:KYH31060.1,
RC ECO:0000313|Proteomes:UP000075531};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium tepidiprofundi DSM 19306.";
RL Submitted (FEB-2016) 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:KYH31060.1}.
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DR EMBL; LTBA01000051; KYH31060.1; -; Genomic_DNA.
DR RefSeq; WP_066827049.1; NZ_LTBA01000051.1.
DR AlphaFoldDB; A0A151AU23; -.
DR STRING; 1121338.CLTEP_24370; -.
DR PATRIC; fig|1121338.3.peg.2519; -.
DR OrthoDB; 9808166at2; -.
DR Proteomes; UP000075531; 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 CDD; cd03280; ABC_MutS2; 1.
DR CDD; cd06503; ATP-synt_Fo_b; 1.
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 NCBIfam; TIGR01069; mutS2; 1.
DR PANTHER; PTHR48378; DNA MISMATCH REPAIR PROTEINS MUTS FAMILY DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR48378:SF2; SMR DOMAIN-CONTAINING PROTEIN; 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; PS00486; DNA_MISMATCH_REPAIR_2; 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};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00092, ECO:0000313|EMBL:KYH31060.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000075531}.
FT DOMAIN 713..788
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT COILED 513..631
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 332..339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ SEQUENCE 788 AA; 88208 MW; 36FC26CD08CA2807 CRC64;
MNKKSLRILE FDKVKERIKK YAQTSAAKDI IDGLEPYDSV FEVRQHLKET DEAFNLLTKK
GNPPFEGLFD VREAINNVGK GATLFPGQLL KIAQLLRSAR RFKSFIAHKE DEEGYPVLED
ICAGIVPLKR IEEKIFNAII GENEIADRAS SKLFNIRKTL REKNSSVKDR VNAMVRSNSK
YLQENLYTIR GDRYVLPVKA EHKSSVPGLV HDQSSSGATL FIEPMSLVNL NNEIKELKLK
EKAEIERILA ELSSDIYDNI NAVRNNANII WELDFIFAKA HYASDLDCIL PIINEDGIID
IIDARHPLID AKEVVPNSIY LGREFTSLVV TGPNTGGKTV TLKTIGIIEI MAMSGLLIPA
KQNSIVSYFD EIFADIGDEQ SIEQSLSTFS SHMTNIVNII DKADDKSLVL FDELGAGTDP
TEGAALAVSI LENLRKRNCK IAATTHYSEL KGYALKTIGV ENASVEFDVE TLRPTYKLLI
GVPGKSNAFE ISRRLGLPEY IISYAKQNIS KDTMEFENLI QSLQDKNIKA EKDAREAEIL
KMDAEKLKNR YAQKLEKLEN IREKAIIEAQ KEAKRVIREA KHEADDILKN IRKLESMGYS
SDVRQKLEKE RKKLKDKLDI AEENLANKSK NKGQKLKSVE EGQEVLLSTI DQKVIVLSKP
DKKGEVLVQA GIMKINVKLD DLRAIKESSS ATSKVNYSKR EAKLNMNMVS SSVDLRGMDS
EEAIYTADKY LDDAYLGGLG EVTIIHGKGT GVLRKAITNM LKKHPHVKSY RIGSYGEGGT
GVTVVELK
//
