ID   MUTL_PORGI              Reviewed;         618 AA.
AC   Q7MX15;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=DNA mismatch repair protein MutL {ECO:0000255|HAMAP-Rule:MF_00149};
GN   Name=mutL {ECO:0000255|HAMAP-Rule:MF_00149}; OrderedLocusNames=PG_0412;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
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; AE015924; AAQ65613.1; -; Genomic_DNA.
DR   RefSeq; WP_005873792.1; NC_002950.2.
DR   AlphaFoldDB; Q7MX15; -.
DR   SMR; Q7MX15; -.
DR   STRING; 242619.PG_0412; -.
DR   EnsemblBacteria; AAQ65613; AAQ65613; PG_0412.
DR   KEGG; pgi:PG_0412; -.
DR   PATRIC; fig|242619.8.peg.376; -.
DR   eggNOG; COG0323; Bacteria.
DR   HOGENOM; CLU_004131_4_0_10; -.
DR   OMA; AHERIMY; -.
DR   OrthoDB; 764332at2; -.
DR   BioCyc; PGIN242619:G1G02-384-MON; -.
DR   Proteomes; UP000000588; Chromosome.
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; Reference proteome.
FT   CHAIN           1..618
FT                   /note="DNA mismatch repair protein MutL"
FT                   /id="PRO_1000058147"
SQ   SEQUENCE   618 AA;  68816 MW;  9278F3A1DE0B73A7 CRC64;
     MSDVIRLLPD SIANQIAAGE VIQRPASVVK ELLENALDAG ASIIRLDVRE AGRELIRVTD
     NGKGMSQSDA RMAFERHATS KIASFQDLFS LRTMGFRGEA LASIAAVAQV ELLTRRAEDE
     LGTRLTINGS EVGEVATVTS PLGCILCVKN LFYNVPARRK FLKSNETEFR HILTEYERVA
     LVNPQVAFSI YHSGELVQDL PPSPLKKRIL DVFGKRMEKD LIPIGMKSPI TNISGFVGRP
     DGARKRGALQ YFFVNGRFMR HPYFHKAVMA AYEAIIPQGT MPNYFLYFDL EPSQIDVNIH
     PTKTEIKFSD EQAIFKLIGV VIREALSSSN AVPAIDFDRK ELIDIPAYQG PGKNVVRPPV
     DLDPSYNPFK ETGLTEPIRS SRRQSPDMGW NELFKQFEAK RDAEKMAEPP IRSEELFAST
     DFTPSAVSAT PSTDMLCYVH RGRYLVTTLS RGLALVDFHR AHKRILYDRF MADESRRHIE
     QQQLLFPELL EFNPSDASAV KAAVDELQSV GFDLSPLGVS SYSLLAAPVQ IIDCAADVVR
     DVIHTTLEDG RSSHEQMLEL IATQIAEYQA IPCGKTPTAE EASDLLAELF ASNDSTYTPD
     GKLIVSIIEE ADIARRFE