ID H3SHG2_9BACL Unreviewed; 785 AA.
AC H3SHG2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=PDENDC454_14877 {ECO:0000313|EMBL:EHQ61498.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ61498.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ61498.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ61498.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(2012).
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:EHQ61498.1}.
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DR EMBL; AHKH01000036; EHQ61498.1; -; Genomic_DNA.
DR RefSeq; WP_006677472.1; NZ_AHKH01000036.1.
DR AlphaFoldDB; H3SHG2; -.
DR STRING; 1131935.PDENDC454_14877; -.
DR PATRIC; fig|1131935.3.peg.3088; -.
DR OrthoDB; 9808166at2; -.
DR Proteomes; UP000003900; 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 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: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; 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:UP000003900}.
FT DOMAIN 710..785
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
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 785 AA; 87238 MW; 08B8920D0A717897 CRC64;
MDSKILNTMD YHKILASLAT HAATGLGEQA ALNLRPSSDL EDVKLRLQAT DEAMTVERLK
GGPPLAGVKD IRGALKRARI QAMLSSTELW DISALLFAAR RTKRHIAAVH EEEAIPLLQD
LAETISDQKQ LEEDIRQCID EQGEILDQAS FELAAIRREL RIGETRIREK LEAMIRSSNA
AKMLQEQLIT IRNDRYVIPV KQEYRSHYGG IVHDQSGSGA TLFIEPEAIV AMNNKLRETK
LREEREIERI LSRLTEQVGL LADVLEYDTG AVETLDFMFA KARLAREMKA SLPRMNDRGF
LKLRKARHPL IPADQVVPID VELGNSYTSI LVTGPNTGGK TVTLKTIGLL NLMAMSGLFI
PAEDGSQMCV FDAIYADIGD EQSIEQSLST FSSHLTNIIR ILEQMTPKSL VLLDEVGAGT
DPAEGSALAI AILEHIHRLG CRMVATTHYS ELKAYAYERK GVINASMEFD VQTLRPTYRL
LVGVPGRSNA FAIAERLGLP KPIIDHARGE VTEEDMRVET MIASLEDNRL KAEAERETAS
KLRMELEAMR QKLSRELEKQ EAEREKRQEQ AEAKARAIVD KARREAQEII AELRQLAMEG
VQVKEHMLTE ARKRLDEAAP EAKLAAKPKR DAKPVRRIEA GDDVRVYSLN QKGSVVELAG
EEAVVQLGIM KMKVPLDDLE LLSSAKSAAK PVQSGANVKR TRGESVRSEL DLRGANLEEA
LMEVDRFLDE ALLGNLGQVY IIHGKGTGIL RSGIQEFLRK HKHVKSFRLG SFGEGGTGVT
VAELK
//
