ID A0A1B8W6M3_9BACI Unreviewed; 788 AA.
AC A0A1B8W6M3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=A7975_14675 {ECO:0000313|EMBL:OBZ12279.1};
OS Bacillus sp. FJAT-26390.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1743142 {ECO:0000313|EMBL:OBZ12279.1, ECO:0000313|Proteomes:UP000092623};
RN [1] {ECO:0000313|EMBL:OBZ12279.1, ECO:0000313|Proteomes:UP000092623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-26390 {ECO:0000313|EMBL:OBZ12279.1,
RC ECO:0000313|Proteomes:UP000092623};
RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Z., Chen Q., Liu B.,
RA Zhu Y., Wang J., Liu G.;
RT "Bacillus sp. FJAT-26390.";
RL Submitted (MAY-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:OBZ12279.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MAQX01000022; OBZ12279.1; -; Genomic_DNA.
DR RefSeq; WP_053374635.1; NZ_MAQX01000022.1.
DR AlphaFoldDB; A0A1B8W6M3; -.
DR Proteomes; UP000092623; 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}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000092623}.
FT DOMAIN 713..788
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT REGION 614..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 522..599
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 334..341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ SEQUENCE 788 AA; 86852 MW; 6A59300CF7453B73 CRC64;
MDTKILKTLE YPKIIHRLSQ HAATSLGKAA AESLQPVSDL EAVKRILQAT DEAYTADRLK
GSAPFGGVVD ISAPLHRARI GGTLNPAELL DIAATARGGR RVKKHISLLH EDNPIPMLHE
VADQISEHKQ LEDAIFECID DQAEVMDSAS AALGSIRREL RNGESRIREK MDQMIRSSTV
QKMLQDSIVT LRNDRYVIPV KQEYRSHFGG IVHDQSGSGA TLFIEPEAIV AMNNKLRELK
AGELREIEKI LQKLTALTSD YVEDLIFNLD LLGQIDFAYA KARLAHSMKA TLPRMNDRGF
LKLKRGRHPL IAPEQVVPID VELGNQYTAI IVTGPNTGGK TVSLKTIGLL SLMAMSGLFV
PAEDGSQLCV FDAIYADIGD EQSIEQSLST FSSHLKNIIR ILSSMTSKSL VLLDELGAGT
DPAEGSALAI AILEHVHAMD SRIVATTHYS ELKAYAYNRK GVINASMEFD VATLSPTYRL
LVGVPGRSNA FAIAERLGLA RSIIEHARGE VSEEDQRVEN MIASLEENRL GAETERQTAE
SLRREMETLR ARHEAERLRF EEQKEKLMLK AQEEAREAVA KAKREAEQII ADLRKLAMEE
GASVKEHKLI EARRKLDEAA PEQQKTKRGG SKTSAKPAKI EAGDEVTVYS LNQKGTVVEV
HGSDATVQLG IMKMKVALDD LELLKSNGAT KVQQPKLAAS LKRSKDDNFK MELDLRGENL
EEAILEVDRF LDEAFLSGLA QVAIIHGKGT GVLRTGIQQY LRRHSHVKSY RLGNYGEGGV
GVTVAELK
//
