ID G9ZT32_9LACO Unreviewed; 788 AA.
AC G9ZT32;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=HMPREF9103_02779 {ECO:0000313|EMBL:EHL95582.1};
OS Lentilactobacillus parafarraginis F0439.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=797515 {ECO:0000313|EMBL:EHL95582.1, ECO:0000313|Proteomes:UP000004625};
RN [1] {ECO:0000313|EMBL:EHL95582.1, ECO:0000313|Proteomes:UP000004625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0439 {ECO:0000313|EMBL:EHL95582.1,
RC ECO:0000313|Proteomes:UP000004625};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) 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:EHL95582.1}.
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DR EMBL; AGEY01000197; EHL95582.1; -; Genomic_DNA.
DR RefSeq; WP_008214877.1; NZ_JH415059.1.
DR AlphaFoldDB; G9ZT32; -.
DR STRING; 797515.HMPREF9103_02779; -.
DR PATRIC; fig|797515.3.peg.2523; -.
DR eggNOG; COG1193; Bacteria.
DR HOGENOM; CLU_011252_2_1_9; -.
DR Proteomes; UP000004625; 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; 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}.
FT DOMAIN 713..788
FT /note="Smr"
FT /evidence="ECO:0000259|PROSITE:PS50828"
FT REGION 690..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 523..600
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 695..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 335..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00092"
SQ SEQUENCE 788 AA; 88008 MW; 2FEBD7D00ACEE95A CRC64;
MNEKVLDTLE YNKIKDQLAG FLTTDRGHEI VQNLQPSGDY AVVDQQLKET ADGADIVRLA
GEIPIPKLTE ISPYMKRLKI ENAALSGTEL AHITKLLRAV KTVSQFFEDF KNEEVTLRTV
PKTVAKLTLM PDITTRMVQS IDDDGRVLDS ASSQLRAIRR TIEQTQSNIR TRMGKYLKGS
ESKYLSEPII TVRDERFVLP IRAEYKSHFG GIVHDQSASG QTLYVEPSNV VEMNNQLRRD
QLAERTEQRR ILAELTEMIR PYRQELLENM NLVGQLDFVN AKAKYAHQSG AVLPKISTEN
VVNLRHARHP LIAKEKVVPN DIKIGADYQT IIVTGPNTGG KTITIKTVGL LQLMGQSGLF
ITADEESQIG VFDDVFADIG DDQSIEANLS TFSSHMDNII AIMKQLTDKS LVLLDELGAG
TDPKEGAALA MAIIDAIHRS GCEMIATTHY PELKAFAYNR PGIINASMEF DVETLRPTYR
LLLGIPGQSN ALNIASRLGM PEQIVQQAKS FTDSENQDIN NMIAELTSQT KRAHDEADEL
ATELSEATKL HADLQKRFDQ YQNQKDRLQE HAREQANEIV EKAKHNADKI IADLHRKQRQ
VGKTTVKENE LIDAKGALNQ LEVAPSLKRN KVLKKEKAKH NFKAGDEVLV KSYGQQGTLI
RQEKNGLWDI QLGILKMQIE EADLEKVGKQ AQPKAKYQTH VSRTRSTGMS PTLDLRGHRY
EEAMYELDRY VDSALLAGYP TITIIHGKGT GALRKGVTDY LKRNSRVKSF GYSAPNAGGD
GSTVVQFK
//
