ID A0A0D5NET6_9BACL Unreviewed; 788 AA.
AC A0A0D5NET6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=VN24_02140 {ECO:0000313|EMBL:AJY73645.1};
OS Paenibacillus beijingensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1126833 {ECO:0000313|EMBL:AJY73645.1, ECO:0000313|Proteomes:UP000032633};
RN [1] {ECO:0000313|EMBL:AJY73645.1, ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|EMBL:AJY73645.1,
RC ECO:0000313|Proteomes:UP000032633};
RX PubMed=25937453; DOI=10.1016/j.jbiotec.2015.04.015;
RA Kwak Y., Shin J.H.;
RT "Complete genome sequence of Paenibacillus beijingensis 7188(T) (=DSM
RT 24997(T)), a novel rhizobacterium from jujube garden soil.";
RL J. Biotechnol. 206:75-76(2015).
RN [2] {ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|Proteomes:UP000032633};
RA Kwak Y., Shin J.-H.;
RT "Genome sequence of Paenibacillus beijingensis strain DSM 24997T.";
RL Submitted (MAR-2015) 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}.
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DR EMBL; CP011058; AJY73645.1; -; Genomic_DNA.
DR RefSeq; WP_045669080.1; NZ_CP011058.1.
DR AlphaFoldDB; A0A0D5NET6; -.
DR STRING; 1126833.VN24_02140; -.
DR KEGG; pbj:VN24_02140; -.
DR PATRIC; fig|1126833.4.peg.469; -.
DR HOGENOM; CLU_011252_2_1_9; -.
DR OrthoDB; 9808166at2; -.
DR Proteomes; UP000032633; Chromosome.
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:UP000032633}.
FT DOMAIN 713..788
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT COILED 229..264
FT /evidence="ECO:0000256|SAM:Coils"
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; 87448 MW; 0D00D48B9275A45F CRC64;
MDDKILQTLE YSKIIHKLLQ HTATTMGRKR AEELRPNSDL EDVKRSLQAT DEASKADRLK
GSAPFGGIAD IAQSLHRARI GGTLNAAELL EIAYTARGAR RVKRHLLQLH EDEPIALLAA
LAQQLAEHRP LEEAIMRCID DSAEVLDSAS MELASIRREL RSGESRIREK LENMIRSTSV
QKMLQDAIIT LRNNRYVIPV KQEYRSHFGG IVHDQSGSGA TLFIEPETIV AMNNKLRELR
AAEEREIEKI LQMLTAQAAE YEEDLLLNSD LLGQLDFAFA KARLAHDMKA ALPRMNDRGF
LKLRRGRHPL IDPQKVVPLD VELGNTHTGI IVTGPNTGGK TVSLKTIGLL SLMAMSGMFV
PAEDGSQLCV FDAIYADIGD EQSIEQSLST FSSHMTNIIR ILRSMTPKSL VLLDELGAGT
DPAEGSALAI AILDHIHRMG CRIVATTHYS ELKAYAYNRK GLINASMEFD VATLSPTYRL
LVGVPGRSNA FAIAERLGLS KMIIDQARGE VSEDDLRVEN MIASLEEDRL SAENERLGAE
AERREMEALR AKYASERLQF EQQRDKLLLK AQEEAREAVA KAKREAEDII ADLRKLAQEE
GAAVKQHKLI EARRKLDEAA PELHKPKKAG AARSVKAVKI EPGDEVMVYS LNQKGHVVDI
SDSEATVQLG IMKMKVKTGD LELIKQAAAI KPQQPKQAAS LKRTRDDNVR MELDLRGSNL
EESIMEVDRF LDESFLSGMG QVYIIHGKGT GVLRSGIQDF LRRHKHVKSY RLGNYGEGGA
GVTVAELK
//
