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Protein

DNA mismatch repair protein MutL

Gene

mutL

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a "molecular matchmaker", a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of the final effector complex. The ATPase activity of MutL is stimulated by DNA.

GO - Molecular functioni

  1. ATPase activity Source: EcoliWiki
  2. ATP binding Source: EcoliWiki
  3. DNA binding Source: EcoliWiki
  4. identical protein binding Source: IntAct
  5. mismatched DNA binding Source: InterPro
  6. single-stranded DNA binding Source: GO_Central

GO - Biological processi

  1. mismatch repair Source: EcoliWiki
  2. regulation of DNA recombination Source: EcoliWiki
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11281-MONOMER.
ECOL316407:JW4128-MONOMER.
MetaCyc:EG11281-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA mismatch repair protein MutL
Gene namesi
Name:mutL
Ordered Locus Names:b4170, JW4128
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11281. mutL.

Subcellular locationi

GO - Cellular componenti

  1. mismatch repair complex Source: EcoliWiki
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 615615DNA mismatch repair protein MutLPRO_0000177943Add
BLAST

Proteomic databases

PaxDbiP23367.
PRIDEiP23367.

Expressioni

Gene expression databases

GenevestigatoriP23367.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-554913,EBI-554913
holAP286302EBI-554913,EBI-549153
holBP286312EBI-554913,EBI-549161
mutHP067228EBI-554913,EBI-545170
recAP0A7G63EBI-554913,EBI-370331
uvrDP030187EBI-554913,EBI-559573
vsrP091843EBI-554913,EBI-765033

Protein-protein interaction databases

DIPiDIP-10285N.
IntActiP23367. 12 interactions.
MINTiMINT-1266937.
STRINGi511145.b4170.

Structurei

Secondary structure

1
615
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 1912Combined sources
Helixi23 – 3614Combined sources
Beta strandi40 – 478Combined sources
Helixi48 – 503Combined sources
Beta strandi52 – 587Combined sources
Helixi65 – 673Combined sources
Helixi68 – 725Combined sources
Helixi83 – 875Combined sources
Helixi90 – 923Combined sources
Helixi98 – 1036Combined sources
Beta strandi106 – 1138Combined sources
Beta strandi115 – 1173Combined sources
Beta strandi118 – 1269Combined sources
Turni127 – 1304Combined sources
Beta strandi131 – 1377Combined sources
Beta strandi141 – 1499Combined sources
Turni150 – 1534Combined sources
Helixi155 – 1595Combined sources
Helixi164 – 18118Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi194 – 1996Combined sources
Helixi209 – 2168Combined sources
Helixi218 – 2236Combined sources
Beta strandi224 – 2318Combined sources
Beta strandi234 – 2418Combined sources
Helixi243 – 2453Combined sources
Helixi250 – 2523Combined sources
Beta strandi254 – 2585Combined sources
Beta strandi261 – 2633Combined sources
Helixi266 – 27914Combined sources
Beta strandi280 – 2823Combined sources
Beta strandi288 – 2936Combined sources
Helixi296 – 2983Combined sources
Beta strandi311 – 3144Combined sources
Helixi315 – 32915Combined sources
Beta strandi437 – 4426Combined sources
Turni443 – 4453Combined sources
Beta strandi446 – 4516Combined sources
Beta strandi454 – 4596Combined sources
Helixi460 – 47213Combined sources
Beta strandi481 – 49111Combined sources
Helixi494 – 50916Combined sources
Beta strandi513 – 5164Combined sources
Beta strandi518 – 52710Combined sources
Helixi528 – 5303Combined sources
Helixi535 – 54612Combined sources
Helixi554 – 56310Combined sources
Helixi574 – 58714Combined sources
Helixi589 – 5935Combined sources
Turni597 – 5993Combined sources
Beta strandi600 – 6023Combined sources
Helixi606 – 6138Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B62X-ray2.10A1-349[»]
1B63X-ray1.90A1-331[»]
1BKNX-ray2.90A/B1-349[»]
1NHHX-ray2.40A1-331[»]
1NHIX-ray2.00A1-331[»]
1NHJX-ray2.30A1-331[»]
1X9ZX-ray2.10A/B432-615[»]
ProteinModelPortaliP23367.
SMRiP23367. Positions 1-331, 433-614.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23367.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0323.
HOGENOMiHOG000256551.
InParanoidiP23367.
KOiK03572.
OMAiFSHIDEI.
OrthoDBiEOG6P8TMH.
PhylomeDBiP23367.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
HAMAPiMF_00149. DNA_mis_repair.
InterProiIPR013507. DNA_mismatch_repair_C.
IPR014762. DNA_mismatch_repair_CS.
IPR002099. DNA_mismatch_repair_fam.
IPR011186. DNA_mismatch_repair_MLH1/HexB.
IPR020667. DNA_mismatch_repair_MutL.
IPR003594. HATPase_C.
IPR014790. MutL_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR10073:SF12. PTHR10073:SF12. 1 hit.
PfamiPF01119. DNA_mis_repair. 1 hit.
PF08676. MutL_C. 1 hit.
[Graphical view]
SMARTiSM00387. HATPase_c. 1 hit.
SM00853. MutL_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
TIGRFAMsiTIGR00585. mutl. 1 hit.
PROSITEiPS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23367-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIQVLPPQL ANQIAAGEVV ERPASVVKEL VENSLDAGAT RIDIDIERGG
60 70 80 90 100
AKLIRIRDNG CGIKKDELAL ALARHATSKI ASLDDLEAII SLGFRGEALA
110 120 130 140 150
SISSVSRLTL TSRTAEQQEA WQAYAEGRDM NVTVKPAAHP VGTTLEVLDL
160 170 180 190 200
FYNTPARRKF LRTEKTEFNH IDEIIRRIAL ARFDVTINLS HNGKIVRQYR
210 220 230 240 250
AVPEGGQKER RLGAICGTAF LEQALAIEWQ HGDLTLRGWV ADPNHTTPAL
260 270 280 290 300
AEIQYCYVNG RMMRDRLINH AIRQACEDKL GADQQPAFVL YLEIDPHQVD
310 320 330 340 350
VNVHPAKHEV RFHQSRLVHD FIYQGVLSVL QQQLETPLPL DDEPQPAPRS
360 370 380 390 400
IPENRVAAGR NHFAEPAARE PVAPRYTPAP ASGSRPAAPW PNAQPGYQKQ
410 420 430 440 450
QGEVYRQLLQ TPAPMQKLKA PEPQEPALAA NSQSFGRVLT IVHSDCALLE
460 470 480 490 500
RDGNISLLSL PVAERWLRQA QLTPGEAPVC AQPLLIPLRL KVSAEEKSAL
510 520 530 540 550
EKAQSALAEL GIDFQSDAQH VTIRAVPLPL RQQNLQILIP ELIGYLAKQS
560 570 580 590 600
VFEPGNIAQW IARNLMSEHA QWSMAQAITL LADVERLCPQ LVKTPPGGLL
610
QSVDLHPAIK ALKDE
Length:615
Mass (Da):67,924
Last modified:May 1, 1992 - v2
Checksum:iC69D2735BF5FA165
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11831 Genomic DNA. Translation: CAA77850.1.
U14003 Genomic DNA. Translation: AAA97066.1.
U00096 Genomic DNA. Translation: AAC77127.1.
AP009048 Genomic DNA. Translation: BAE78171.1.
M63655 Genomic DNA. Translation: AAA24173.1.
L19346 Unassigned DNA. Translation: AAA20098.1.
PIRiPH0853.
RefSeqiNP_418591.1. NC_000913.3.
YP_492312.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77127; AAC77127; b4170.
BAE78171; BAE78171; BAE78171.
GeneIDi12934482.
948691.
KEGGiecj:Y75_p4056.
eco:b4170.
PATRICi32123913. VBIEscCol129921_4301.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11831 Genomic DNA. Translation: CAA77850.1.
U14003 Genomic DNA. Translation: AAA97066.1.
U00096 Genomic DNA. Translation: AAC77127.1.
AP009048 Genomic DNA. Translation: BAE78171.1.
M63655 Genomic DNA. Translation: AAA24173.1.
L19346 Unassigned DNA. Translation: AAA20098.1.
PIRiPH0853.
RefSeqiNP_418591.1. NC_000913.3.
YP_492312.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B62X-ray2.10A1-349[»]
1B63X-ray1.90A1-331[»]
1BKNX-ray2.90A/B1-349[»]
1NHHX-ray2.40A1-331[»]
1NHIX-ray2.00A1-331[»]
1NHJX-ray2.30A1-331[»]
1X9ZX-ray2.10A/B432-615[»]
ProteinModelPortaliP23367.
SMRiP23367. Positions 1-331, 433-614.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10285N.
IntActiP23367. 12 interactions.
MINTiMINT-1266937.
STRINGi511145.b4170.

Proteomic databases

PaxDbiP23367.
PRIDEiP23367.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77127; AAC77127; b4170.
BAE78171; BAE78171; BAE78171.
GeneIDi12934482.
948691.
KEGGiecj:Y75_p4056.
eco:b4170.
PATRICi32123913. VBIEscCol129921_4301.

Organism-specific databases

EchoBASEiEB1258.
EcoGeneiEG11281. mutL.

Phylogenomic databases

eggNOGiCOG0323.
HOGENOMiHOG000256551.
InParanoidiP23367.
KOiK03572.
OMAiFSHIDEI.
OrthoDBiEOG6P8TMH.
PhylomeDBiP23367.

Enzyme and pathway databases

BioCyciEcoCyc:EG11281-MONOMER.
ECOL316407:JW4128-MONOMER.
MetaCyc:EG11281-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP23367.
PROiP23367.

Gene expression databases

GenevestigatoriP23367.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
HAMAPiMF_00149. DNA_mis_repair.
InterProiIPR013507. DNA_mismatch_repair_C.
IPR014762. DNA_mismatch_repair_CS.
IPR002099. DNA_mismatch_repair_fam.
IPR011186. DNA_mismatch_repair_MLH1/HexB.
IPR020667. DNA_mismatch_repair_MutL.
IPR003594. HATPase_C.
IPR014790. MutL_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR10073:SF12. PTHR10073:SF12. 1 hit.
PfamiPF01119. DNA_mis_repair. 1 hit.
PF08676. MutL_C. 1 hit.
[Graphical view]
SMARTiSM00387. HATPase_c. 1 hit.
SM00853. MutL_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
TIGRFAMsiTIGR00585. mutl. 1 hit.
PROSITEiPS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nonconserved segment of the MutL protein from Escherichia coli K-12 and Salmonella typhimurium."
    Tsui H.-C.T., Mandavilli B.S., Winkler M.E.
    Nucleic Acids Res. 20:2379-2379(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Structure of Escherichia coli K-12 miaA and characterization of the mutator phenotype caused by miaA insertion mutations."
    Winkler M.E., Connolly D.M.
    J. Bacteriol. 173:1711-1721(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 596-615.
    Strain: K12.
  6. "The mutL repair gene of Escherichia coli K-12 forms a superoperon with a gene encoding a new cell-wall amidase."
    Tsui H.-C.T., Zhao G., Feng G., Leung H.-C.E., Winkler M.E.
    Mol. Microbiol. 11:189-202(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
    Strain: K12.
  7. "Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis."
    Ban C., Yang W.
    Cell 95:541-552(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-349.
  8. "Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair."
    Ban C., Junop M., Yang W.
    Cell 97:85-97(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-349.
    Strain: K12.

Entry informationi

Entry nameiMUTL_ECOLI
AccessioniPrimary (citable) accession number: P23367
Secondary accession number(s): Q2M6D5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: May 1, 1992
Last modified: March 4, 2015
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.