MUTL_TREPA
ID MUTL_TREPA Reviewed; 620 AA.
AC O83325;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=DNA mismatch repair protein MutL;
GN Name=mutL; OrderedLocusNames=TP_0303;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC65291.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000520; AAC65291.1; ALT_INIT; Genomic_DNA.
DR PIR; A71342; A71342.
DR AlphaFoldDB; O83325; -.
DR SMR; O83325; -.
DR IntAct; O83325; 1.
DR STRING; 243276.TPANIC_0303; -.
DR EnsemblBacteria; AAC65291; AAC65291; TP_0303.
DR KEGG; tpa:TP_0303; -.
DR eggNOG; COG0323; Bacteria.
DR HOGENOM; CLU_004131_4_1_12; -.
DR OMA; AHERIMY; -.
DR Proteomes; UP000000811; 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..620
FT /note="DNA mismatch repair protein MutL"
FT /id="PRO_0000177988"
FT REGION 360..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 68496 MW; 0604AD802671EA36 CRC64;
MHETSYKPIH RLSPDTAKKI AAGEVIERPA SVVRELLENA LDAGATKIHL EINAGGCALI
RVSDNGHGMS PQDLLLCAEA HTTSKISSAD DLLQLRTLGF RGEALASIAA VSRLHLTSTR
SGPLAWHYQP KAAGTAAHVP PVPQGTEAGV LEPASLERGT VVRVEQLFEN FPARKRFLGR
QSAETTLCRS ALIDVSLAHH PVEFRFTVDG THKLTLLSQQ TRKDRCLETQ MLKGDPALFH
TIEGGDCSFH FHLVLSEPAI CRRERRGIFT FVNGRRIFDY GLVQALVLGS EGYFPNGTFP
VACLFLTVNS ERIDFNIHPA KKEVHLQDYA HIRHTLSRSV AHFYRQCTIA HYVRAEPAHA
PATQGNAPTH SSPPCTGVRE EPAAPCAHTP RYESLFPLPV QHAHLLPPSP PHISCEHARD
CTHPAPAAEG DAPVHNHTHT GAFKVLGQVA GTFIAVERNN ALYLIDQHAA HERIIFDTLQ
RNLGTAQILL IPYHIHPRSD EEARIMHRAC TELSPAGFRF HEEPDGSWHV TAVPLHWRGS
EEQLAHDILY SGKNAHDILR HVLATCACRS ACKDGTILDD ATLHSLVEQA FALPQSRCPH
GRPIWIVIGR DELFKRIKRT