MUTL_ECOLI
ID MUTL_ECOLI Reviewed; 615 AA.
AC P23367; Q2M6D5;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=DNA mismatch repair protein MutL;
GN Name=mutL; OrderedLocusNames=b4170, JW4128;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1594459; DOI=10.1093/nar/20.9.2379;
RA Tsui H.-C.T., Mandavilli B.S., Winkler M.E.;
RT "Nonconserved segment of the MutL protein from Escherichia coli K-12 and
RT Salmonella typhimurium.";
RL Nucleic Acids Res. 20:2379-2379(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 596-615.
RC STRAIN=K12;
RX PubMed=1999389; DOI=10.1128/jb.173.5.1711-1721.1991;
RA Winkler M.E., Connolly D.M.;
RT "Structure of Escherichia coli K-12 miaA and characterization of the
RT mutator phenotype caused by miaA insertion mutations.";
RL J. Bacteriol. 173:1711-1721(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RC STRAIN=K12;
RX PubMed=7511774; DOI=10.1111/j.1365-2958.1994.tb00300.x;
RA Tsui H.-C.T., Zhao G., Feng G., Leung H.-C.E., Winkler M.E.;
RT "The mutL repair gene of Escherichia coli K-12 forms a superoperon with a
RT gene encoding a new cell-wall amidase.";
RL Mol. Microbiol. 11:189-202(1994).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-349.
RX PubMed=9827806; DOI=10.1016/s0092-8674(00)81621-9;
RA Ban C., Yang W.;
RT "Crystal structure and ATPase activity of MutL: implications for DNA repair
RT and mutagenesis.";
RL Cell 95:541-552(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-349.
RC STRAIN=K12;
RX PubMed=10199405; DOI=10.1016/s0092-8674(00)80717-5;
RA Ban C., Junop M., Yang W.;
RT "Transformation of MutL by ATP binding and hydrolysis: a switch in DNA
RT mismatch repair.";
RL Cell 97:85-97(1999).
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 the final
CC effector complex. The ATPase activity of MutL is stimulated by DNA.
CC -!- INTERACTION:
CC P23367; P06710-2: dnaX; NbExp=2; IntAct=EBI-554913, EBI-2604194;
CC P23367; P28630: holA; NbExp=2; IntAct=EBI-554913, EBI-549153;
CC P23367; P28631: holB; NbExp=2; IntAct=EBI-554913, EBI-549161;
CC P23367; P06722: mutH; NbExp=8; IntAct=EBI-554913, EBI-545170;
CC P23367; P23367: mutL; NbExp=4; IntAct=EBI-554913, EBI-554913;
CC P23367; P23909: mutS; NbExp=4; IntAct=EBI-554913, EBI-554920;
CC P23367; P0A7G6: recA; NbExp=3; IntAct=EBI-554913, EBI-370331;
CC P23367; P03018: uvrD; NbExp=7; IntAct=EBI-554913, EBI-559573;
CC P23367; P09184: vsr; NbExp=3; IntAct=EBI-554913, EBI-765033;
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000305}.
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DR EMBL; Z11831; CAA77850.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97066.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77127.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78171.1; -; Genomic_DNA.
DR EMBL; M63655; AAA24173.1; -; Genomic_DNA.
DR EMBL; L19346; AAA20098.1; -; Unassigned_DNA.
DR PIR; PH0853; PH0853.
DR RefSeq; NP_418591.1; NC_000913.3.
DR RefSeq; WP_001122505.1; NZ_STEB01000013.1.
DR PDB; 1B62; X-ray; 2.10 A; A=1-349.
DR PDB; 1B63; X-ray; 1.90 A; A=1-331.
DR PDB; 1BKN; X-ray; 2.90 A; A/B=1-349.
DR PDB; 1NHH; X-ray; 2.40 A; A=1-331.
DR PDB; 1NHI; X-ray; 2.00 A; A=1-331.
DR PDB; 1NHJ; X-ray; 2.30 A; A=1-331.
DR PDB; 1X9Z; X-ray; 2.10 A; A/B=432-615.
DR PDB; 5AKB; X-ray; 4.71 A; C/D/F=1-349.
DR PDB; 5AKC; X-ray; 6.60 A; C/D/G/H/K/L=1-349.
DR PDB; 5AKD; X-ray; 7.60 A; C/D/G/H/K/L=1-349.
DR PDB; 6E8E; X-ray; 2.25 A; A/B=466-569.
DR PDB; 7AIB; EM; 4.70 A; C=1-331.
DR PDB; 7AIC; EM; 5.00 A; C=1-331.
DR PDBsum; 1B62; -.
DR PDBsum; 1B63; -.
DR PDBsum; 1BKN; -.
DR PDBsum; 1NHH; -.
DR PDBsum; 1NHI; -.
DR PDBsum; 1NHJ; -.
DR PDBsum; 1X9Z; -.
DR PDBsum; 5AKB; -.
DR PDBsum; 5AKC; -.
DR PDBsum; 5AKD; -.
DR PDBsum; 6E8E; -.
DR PDBsum; 7AIB; -.
DR PDBsum; 7AIC; -.
DR AlphaFoldDB; P23367; -.
DR SMR; P23367; -.
DR BioGRID; 4263476; 52.
DR BioGRID; 852983; 2.
DR ComplexPortal; CPX-5541; MutHLS methyl-directed mismatch repair complex.
DR ComplexPortal; CPX-5542; MutL-UvrD DNA helicase complex.
DR DIP; DIP-10285N; -.
DR IntAct; P23367; 14.
DR STRING; 511145.b4170; -.
DR DrugBank; DB09462; Glycerin.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR jPOST; P23367; -.
DR PaxDb; P23367; -.
DR PRIDE; P23367; -.
DR EnsemblBacteria; AAC77127; AAC77127; b4170.
DR EnsemblBacteria; BAE78171; BAE78171; BAE78171.
DR GeneID; 948691; -.
DR KEGG; ecj:JW4128; -.
DR KEGG; eco:b4170; -.
DR PATRIC; fig|1411691.4.peg.2531; -.
DR EchoBASE; EB1258; -.
DR eggNOG; COG0323; Bacteria.
DR HOGENOM; CLU_004131_5_1_6; -.
DR InParanoid; P23367; -.
DR OMA; ATQEQAW; -.
DR PhylomeDB; P23367; -.
DR BioCyc; EcoCyc:EG11281-MON; -.
DR BioCyc; MetaCyc:EG11281-MON; -.
DR EvolutionaryTrace; P23367; -.
DR PRO; PR:P23367; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032300; C:mismatch repair complex; IBA:GO_Central.
DR GO; GO:0017117; C:single-stranded DNA-dependent ATP-dependent DNA helicase complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IDA:EcoliWiki.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoliWiki.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0006298; P:mismatch repair; IDA:EcoliWiki.
DR GO; GO:0070716; P:mismatch repair involved in maintenance of fidelity involved in DNA-dependent DNA replication; IDA:ComplexPortal.
DR GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; IDA:ComplexPortal.
DR GO; GO:0000018; P:regulation of DNA recombination; IMP:EcoliWiki.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA repair; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..615
FT /note="DNA mismatch repair protein MutL"
FT /id="PRO_0000177943"
FT REGION 363..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 8..19
FT /evidence="ECO:0007829|PDB:1B63"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:1B63"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:1B63"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1B63"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:1B63"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:1B63"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1BKN"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1BKN"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:1B63"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:1B63"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:1B63"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:1B63"
FT HELIX 164..181
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:1B63"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:1B63"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 234..241
FT /evidence="ECO:0007829|PDB:1B63"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1B63"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1NHI"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:1B63"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:1NHJ"
FT HELIX 315..329
FT /evidence="ECO:0007829|PDB:1B63"
FT STRAND 437..442
FT /evidence="ECO:0007829|PDB:1X9Z"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:1X9Z"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:1X9Z"
FT STRAND 454..459
FT /evidence="ECO:0007829|PDB:1X9Z"
FT HELIX 460..472
FT /evidence="ECO:0007829|PDB:1X9Z"
FT STRAND 481..491
FT /evidence="ECO:0007829|PDB:1X9Z"
FT HELIX 494..509
FT /evidence="ECO:0007829|PDB:1X9Z"
FT STRAND 513..516
FT /evidence="ECO:0007829|PDB:1X9Z"
FT STRAND 518..527
FT /evidence="ECO:0007829|PDB:1X9Z"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:1X9Z"
FT HELIX 535..546
FT /evidence="ECO:0007829|PDB:1X9Z"
FT HELIX 554..563
FT /evidence="ECO:0007829|PDB:1X9Z"
FT HELIX 574..587
FT /evidence="ECO:0007829|PDB:1X9Z"
FT HELIX 589..593
FT /evidence="ECO:0007829|PDB:1X9Z"
FT TURN 597..599
FT /evidence="ECO:0007829|PDB:1X9Z"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:1X9Z"
FT HELIX 606..613
FT /evidence="ECO:0007829|PDB:1X9Z"
SQ SEQUENCE 615 AA; 67924 MW; C69D2735BF5FA165 CRC64;
MPIQVLPPQL ANQIAAGEVV ERPASVVKEL VENSLDAGAT RIDIDIERGG AKLIRIRDNG
CGIKKDELAL ALARHATSKI ASLDDLEAII SLGFRGEALA SISSVSRLTL TSRTAEQQEA
WQAYAEGRDM NVTVKPAAHP VGTTLEVLDL FYNTPARRKF LRTEKTEFNH IDEIIRRIAL
ARFDVTINLS HNGKIVRQYR AVPEGGQKER RLGAICGTAF LEQALAIEWQ HGDLTLRGWV
ADPNHTTPAL AEIQYCYVNG RMMRDRLINH AIRQACEDKL GADQQPAFVL YLEIDPHQVD
VNVHPAKHEV RFHQSRLVHD FIYQGVLSVL QQQLETPLPL DDEPQPAPRS IPENRVAAGR
NHFAEPAARE PVAPRYTPAP ASGSRPAAPW PNAQPGYQKQ QGEVYRQLLQ TPAPMQKLKA
PEPQEPALAA NSQSFGRVLT IVHSDCALLE RDGNISLLSL PVAERWLRQA QLTPGEAPVC
AQPLLIPLRL KVSAEEKSAL EKAQSALAEL GIDFQSDAQH VTIRAVPLPL RQQNLQILIP
ELIGYLAKQS VFEPGNIAQW IARNLMSEHA QWSMAQAITL LADVERLCPQ LVKTPPGGLL
QSVDLHPAIK ALKDE
