ID   MUTL_STRTD              Reviewed;         647 AA.
AC   Q03MY0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=DNA mismatch repair protein MutL {ECO:0000255|HAMAP-Rule:MF_00149};
GN   Name=mutL {ECO:0000255|HAMAP-Rule:MF_00149}; OrderedLocusNames=STER_0072;
OS   Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=322159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-491 / LMD-9;
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; CP000419; ABJ65442.1; -; Genomic_DNA.
DR   RefSeq; WP_011680601.1; NC_008532.1.
DR   AlphaFoldDB; Q03MY0; -.
DR   SMR; Q03MY0; -.
DR   KEGG; ste:STER_0072; -.
DR   HOGENOM; CLU_004131_4_1_9; -.
DR   OMA; AHERIMY; -.
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; 2.
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..647
FT                   /note="DNA mismatch repair protein MutL"
FT                   /id="PRO_1000010097"
FT   REGION          389..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..405
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   647 AA;  72479 MW;  4B59F7B1E053AF85 CRC64;
     MPKIIELPEV LANQIAAGEV VERPASVVKE LVENAIDAGS TQITIEVEES GLSKIQITDN
     GEGMAQADVA MSLRRHATSK IKNQGDLFRI RTLGFRGEAL PSIASISHLT IVTAADGEVY
     GTKLVAKGGE IESQDPISTP VGTKITVENL FYNTPARLKY MKSLQAELAH IVDVVNRLSL
     AHPEVAFTLL NDGRQLTQTS GTGDLRQAIA GIYGLTTAKK MVEISNSDLD FEVSGYVSLP
     ELTRANRNYI TILINGRYIK NFLLNRAIFD GYGSKLMVGR FPIAVIDIQI DPYLADVNVH
     PTKQEVRISK EKELMALIKS AIAQSLREQD LIPDALENLA KSSTRGATRS VQTSLPLKQT
     NLYYDSSRND FFVTPETVQE DIKPLVSKSE SSVSSVANKQ QPTVKQAKRS ADDSDSEHGK
     LDYKNKSKLK RMLENLTNEE TSTFPELEFF GQMHGTYLFA QGQGGLYIID QHAAQERVKY
     EYYREKIGVV DSSLQQLLVP YLFEFSGSDY ISLQEKMPLL NQVCIYLEPY GNNTFILREH
     PIWMKEEEIE SAVYEMCDML LLTNEVSVKT YRAELAIMMS CKRSIKANHA LDDYSARDLL
     VQLAQCKNPY NCPHGRPVLV NFTKSDMEKM FRRIQENHTS LRDLGKY