ID   MUTL_LACDB              Reviewed;         653 AA.
AC   Q048Y5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=DNA mismatch repair protein MutL {ECO:0000255|HAMAP-Rule:MF_00149};
GN   Name=mutL {ECO:0000255|HAMAP-Rule:MF_00149}; OrderedLocusNames=LBUL_1494;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365 / Lb-18).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=321956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-365 / Lb-18;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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:0000255|HAMAP-Rule:MF_00149}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC       {ECO:0000255|HAMAP-Rule:MF_00149}.
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DR   EMBL; CP000412; ABJ58987.1; -; Genomic_DNA.
DR   RefSeq; WP_011678484.1; NC_008529.1.
DR   AlphaFoldDB; Q048Y5; -.
DR   SMR; Q048Y5; -.
DR   KEGG; lbu:LBUL_1494; -.
DR   HOGENOM; CLU_004131_4_2_9; -.
DR   OMA; AHERIMY; -.
DR   BioCyc; LDEL321956:LBUL_RS07060-MON; -.
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   Gene3D; 3.30.1370.100; -; 1.
DR   Gene3D; 3.30.1540.20; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 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; IPR002099; DNA_mismatch_repair_N.
DR   InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR038973; MutL/Mlh/Pms.
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_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10073; PTHR10073; 1.
DR   Pfam; PF01119; DNA_mis_repair; 1.
DR   Pfam; PF08676; MutL_C; 1.
DR   SMART; SM01340; DNA_mis_repair; 1.
DR   SMART; SM00853; MutL_C; 1.
DR   SUPFAM; SSF118116; SSF118116; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00585; mutl; 1.
DR   PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair.
FT   CHAIN           1..653
FT                   /note="DNA mismatch repair protein MutL"
FT                   /id="PRO_1000010031"
FT   REGION          368..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   653 AA;  72356 MW;  45216F6D5D0F9667 CRC64;
     MAKIHELSEN LTNQIAAGEV IERPASVVKE LVENAIDAQA SRIRVEVQHS GLKQISVQDN
     GSGIAPDQVD LAFMRHATSK IQDEHDLFNI ATLGFRGEAL ASIAAVAHVE ILTSTGGQTA
     TRAAFAGGVK KFQEDAGSAK GTKITVGDIF YNTPARLKYL KSPKTELLKI VDIVNRIALG
     HPEISLTLAS DGKVLLRTPG NGNLKQDVAN IYGRKVAEKM LTVENEDPDF TLYGLVSEAN
     LTRSSRNFIS ILLNGRYIKN YQLSSALLDG YGNKLGGKYP IAVLAIEADP LLVDVNVHPT
     KEEVRLSKEK ELSRLITSAV TEALMDEDEA SPLFQLTPFK DKTQLDQLEF NLKPNVVDTR
     RPDDFQLEVS QVAEPEGKTD ITNKKGTETK EKAEKKENKQ EEKEEKTSAP EYVDLNQVRE
     DDQYVLTKSW DQHVKEQTAL PPFAGGEEAA SPVTSKADQL LRQHLPALRL LGQMEGYLLA
     EHGGDLYLID QVAARRRLEY DQILASLEKD ENYQQGLLEP LVFDFSVYDY QKLKDQLPLL
     RQLGLEMEDF GQNTLLMHSY PTWLKGEVTV QVRELLDQLL SSRENDGKSL LKLVAAKAAE
     SNVSRRVNLT GAEAADLLLR LQTASDPYRD ASGQVAVVRL SQNDLSKLFK KGK