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Database: UniProt
Entry: A0A098EZQ8_9BACI
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ID   A0A098EZQ8_9BACI        Unreviewed;       660 AA.
AC   A0A098EZQ8;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=DNA mismatch repair protein MutL {ECO:0000256|HAMAP-Rule:MF_00149};
GN   Name=mutL {ECO:0000256|HAMAP-Rule:MF_00149};
GN   ORFNames=BN1002_01734 {ECO:0000313|EMBL:CEG26882.1};
OS   Bacillus sp. B-jedd.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1476857 {ECO:0000313|EMBL:CEG26882.1, ECO:0000313|Proteomes:UP000042335};
RN   [1] {ECO:0000313|EMBL:CEG26882.1, ECO:0000313|Proteomes:UP000042335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-jedd {ECO:0000313|EMBL:CEG26882.1,
RC   ECO:0000313|Proteomes:UP000042335};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein is involved in the repair of mismatches in DNA.
CC       It is required for dam-dependent methyl-directed DNA mismatch repair.
CC       May act as a 'molecular matchmaker', a protein that promotes the
CC       formation of a stable complex between two or more DNA-binding proteins
CC       in an ATP-dependent manner without itself being part of a final
CC       effector complex. {ECO:0000256|HAMAP-Rule:MF_00149}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC       {ECO:0000256|ARBA:ARBA00006082, ECO:0000256|HAMAP-Rule:MF_00149}.
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DR   EMBL; CCXR01000001; CEG26882.1; -; Genomic_DNA.
DR   RefSeq; WP_048824537.1; NZ_CCXR01000001.1.
DR   AlphaFoldDB; A0A098EZQ8; -.
DR   STRING; 1476857.BN1002_01734; -.
DR   OrthoDB; 9763467at2; -.
DR   Proteomes; UP000042335; Unassembled WGS sequence.
DR   GO; GO:0032300; C:mismatch repair complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0006298; P:mismatch repair; IEA:UniProtKB-UniRule.
DR   CDD; cd16926; HATPase_MutL-MLH-PMS-like; 1.
DR   CDD; cd00782; MutL_Trans; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.1540.20; MutL, C-terminal domain, dimerisation subdomain; 1.
DR   Gene3D; 3.30.1370.100; MutL, C-terminal domain, regulatory subdomain; 1.
DR   HAMAP; MF_00149; DNA_mis_repair; 1.
DR   InterPro; IPR014762; DNA_mismatch_repair_CS.
DR   InterPro; IPR020667; DNA_mismatch_repair_MutL.
DR   InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR002099; MutL/Mlh/PMS.
DR   InterPro; IPR038973; MutL/Mlh/Pms-like.
DR   InterPro; IPR014790; MutL_C.
DR   InterPro; IPR042120; MutL_C_dimsub.
DR   InterPro; IPR042121; MutL_C_regsub.
DR   InterPro; IPR037198; MutL_C_sf.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00585; mutl; 1.
DR   PANTHER; PTHR10073; DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL; 1.
DR   PANTHER; PTHR10073:SF12; DNA MISMATCH REPAIR PROTEIN MLH1; 1.
DR   Pfam; PF01119; DNA_mis_repair; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF08676; MutL_C; 1.
DR   SMART; SM01340; DNA_mis_repair; 1.
DR   SMART; SM00853; MutL_C; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF118116; DNA mismatch repair protein MutL; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00149};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00149}; Reference proteome {ECO:0000313|Proteomes:UP000042335}.
FT   DOMAIN          208..326
FT                   /note="DNA mismatch repair protein S5"
FT                   /evidence="ECO:0000259|SMART:SM01340"
FT   DOMAIN          474..616
FT                   /note="MutL C-terminal dimerisation"
FT                   /evidence="ECO:0000259|SMART:SM00853"
FT   REGION          334..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..384
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   660 AA;  73528 MW;  4B70887DC92A1C49 CRC64;
     MGKIIQLDDA LSNKIAAGEV VERPASVVKE LVENSLDAGS TIIEIEVEEA GLAKIRITDN
     GDGIEEDDVT KAFHRHATSK IKDEADLFRI RTLGFRGEAL PSIASVSRLE MKTSTGESAG
     TRIVVEGGKE TVFEKASSRR GTDIIVTDLF FNTPARLKYV KTIHTELGNI SDLVNRLALS
     HPEVSFRLIH NGKKLLHTNG NGDVRQVLAA IYGMGIAKML VPIEGRSLDY RISGFASLPE
     VTRASRNYIS TMINGRFIKN YGLAKAVMEG YHTLLPIGRF PIVLMNIEMD PILVDVNVHP
     SKMEVRISKE AELYELVRNT IAASFKKRQL IPSGAKPLKT EKPKSEQTSL ELDGSSAVSA
     NSQANEERAG QPVRTEERNE AVSRYEEPST VVVSRPGISS RIAGSTEGSR GIPPRKSEAE
     WASFPSQVKE ILLPKEEPSD LGQVPDDLGS DASRMETAGS ESVGQAERVP GMYPIGQMHG
     TYILAQNENG LYIIDQHAAQ ERIKYEFFRE KVGQVENELQ DMLVPLTFEY STDECLKINE
     YKDELEKVGV FLEDFGPNSF IIRSHPQWLP HGEEQEIIEE MIEQLLSMKK VDIKKLREEA
     AIMMSCKGSI KANHYLRNDE IQALLDELRL ASDPFTCPHG RPIIVHFSSY EMEKMFKRVM
//
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