ID   MUTL_BORBU              Reviewed;         610 AA.
AC   O51229;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=DNA mismatch repair protein MutL;
GN   Name=mutL; OrderedLocusNames=BB_0211;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC       {ECO:0000305}.
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DR   EMBL; AE000783; AAC66594.1; -; Genomic_DNA.
DR   PIR; C70126; C70126.
DR   RefSeq; NP_212345.1; NC_001318.1.
DR   RefSeq; WP_002656028.1; NC_001318.1.
DR   AlphaFoldDB; O51229; -.
DR   SMR; O51229; -.
DR   STRING; 224326.BB_0211; -.
DR   PRIDE; O51229; -.
DR   EnsemblBacteria; AAC66594; AAC66594; BB_0211.
DR   KEGG; bbu:BB_0211; -.
DR   PATRIC; fig|224326.49.peg.608; -.
DR   HOGENOM; CLU_004131_4_1_12; -.
DR   OMA; AHERIMY; -.
DR   Proteomes; UP000001807; 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; 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; Reference proteome.
FT   CHAIN           1..610
FT                   /note="DNA mismatch repair protein MutL"
FT                   /id="PRO_0000177928"
SQ   SEQUENCE   610 AA;  71543 MW;  36A41A8A884EC9FA CRC64;
     MNKIRFLDKY LVQKIAAGES IDRPCSILRE LLDNSIDSGA TKIEVFLEEG GIQKILIIDN
     GSGISKEDLK ICYLPHTTSK ISSEEDLRKI ETLGFRGEAL SSIAICSNIS ITSSTTSNES
     YQIEVENGIE KCFKKQPAIN GTIVDVTKIF HNFPARKRFL KQEPIETKMC LKVLEEKIIT
     HPEINFEINL NQKLRKIYFK ESLIDRVQNV YGNVIENNKF RVLKKEHDNI KIEIFLAPDN
     FSKKSKRHIK TFVNRRPIDQ KDLLEAITNG HSRILSPGNF PICYLFLEIN PEYIDFNVHP
     QKKEVRFYNL PFLFKLISDN INNFFDKNIN NYQDIIIKRQ LTEDDHLIEM TNQPENFNKI
     NTYDIPQNNN LETEDVNEPN KNTTQSNIDL RRYNSIIQNR PTLRENIGNI FSDNFLEFEE
     PPNKNEKEEI KFNYIGQIFS EFLIVEKINE IYFIDQHAVH EKIIYEKLRN SKKNVQKLLV
     PIEFTVVDKN IEEIIDSEIE EYKQMDIIIS KIGPKKYQLE SIPNICSQYE NTLINFFQSR
     RSRTINSLES DLYATIACRK AVKRNDMLSA EFSKFLINEF FKLEIKHCPH GRKIYYKISK
     FELEKKVDRA