ID A0A0R1JRN8_9LACO Unreviewed; 784 AA.
AC A0A0R1JRN8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=FD02_GL000393 {ECO:0000313|EMBL:KRK70330.1};
OS Lacticaseibacillus nasuensis JCM 17158.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1291734 {ECO:0000313|EMBL:KRK70330.1, ECO:0000313|Proteomes:UP000051804};
RN [1] {ECO:0000313|EMBL:KRK70330.1, ECO:0000313|Proteomes:UP000051804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17158 {ECO:0000313|EMBL:KRK70330.1,
RC ECO:0000313|Proteomes:UP000051804};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRK70330.1}.
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DR EMBL; AZDJ01000032; KRK70330.1; -; Genomic_DNA.
DR RefSeq; WP_054722463.1; NZ_BBAM01000015.1.
DR AlphaFoldDB; A0A0R1JRN8; -.
DR STRING; 1291734.FD02_GL000393; -.
DR PATRIC; fig|1291734.4.peg.407; -.
DR OrthoDB; 9808166at2; -.
DR Proteomes; UP000051804; 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:UP000051804}.
FT DOMAIN 709..784
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT COILED 514..598
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 333..340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ SEQUENCE 784 AA; 85162 MW; E0BCAE73461A5D94 CRC64;
MNTKILQTLE FDKIRQALRA NVVTANGDAR AAALTPSADV ATVRETLAET SDGAAILRLT
GGIPVPALTD ITPALQRVRI GAVLNGKELA AVTRVLKTVQ AVSDFFADLA ERLEADTVAA
LAAQLTALPA LTRTLRKAVD EDGRLTDEAS PELGRIRGQV RQLENTIRSR MEQYTRGNSA
KYLSDPIITI RDDRYVIPVK AEHRSQFGGV VHDQSASGQT LFVEPQAIVD MNNRLREAQI
AEQTESERIL AELSNEVAPY ASELRQNADI LGHLDFINAK AKYAKTIKAT APEVSAENHV
DLLAARHPLL DPAKVVPNRI TLGADYGAIV VTGPNTGGKT ITLKTLGLLQ LMGQAGLFIP
AEAGSQIGVY SNVFADIGDE QSIEQSLSTF SGHMKTIVDI LDQLDARSLV LFDELGAGTD
PQEGAALAIA ILDEVGASGA AVVATTHYPE LKLYGYNTPG TINASMEFDS NTLQPTYRLL
IGVPGRSNAF DISLRLGLAA PIVERAKGLI ADDSHDLNNM IADLENQRKA AETEYHETRR
QLAEAEQLHA DLQHAYEQFY AEREHQLAIA KDKANALVDT AQAKADKIIK QLRQLQLAQH
SDIKENQLIE AKTALNNLHQ SKPVKQNRVL RREKAKQSLR QGDTVKSLQY GQTGTLMKQV
DKTHWEVQLG IIRMQLPTSD LQKVTQASEP EPKRRITTVR GASGPSTTLD LRGERYEAAM
AKLDQYIDAA LLAGYPQVTI IHGLGTGAIR NGVTKYLRQN KQVAKFGFAP QNAGGGGATI
VQFK
//
