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P23367

- MUTL_ECOLI

UniProt

P23367 - MUTL_ECOLI

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Protein

DNA mismatch repair protein MutL

Gene

mutL

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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: RefGenome

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. mismatch repair Source: EcoliWiki
  3. 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: Chromosome, UP000000625: 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 – 1912
Helixi23 – 3614
Beta strandi40 – 478
Helixi48 – 503
Beta strandi52 – 587
Helixi65 – 673
Helixi68 – 725
Helixi83 – 875
Helixi90 – 923
Helixi98 – 1036
Beta strandi106 – 1138
Beta strandi115 – 1173
Beta strandi118 – 1269
Turni127 – 1304
Beta strandi131 – 1377
Beta strandi141 – 1499
Turni150 – 1534
Helixi155 – 1595
Helixi164 – 18118
Beta strandi186 – 1916
Beta strandi194 – 1996
Helixi209 – 2168
Helixi218 – 2236
Beta strandi224 – 2318
Beta strandi234 – 2418
Helixi243 – 2453
Helixi250 – 2523
Beta strandi254 – 2585
Beta strandi261 – 2633
Helixi266 – 27914
Beta strandi280 – 2823
Beta strandi288 – 2936
Helixi296 – 2983
Beta strandi311 – 3144
Helixi315 – 32915
Beta strandi437 – 4426
Turni443 – 4453
Beta strandi446 – 4516
Beta strandi454 – 4596
Helixi460 – 47213
Beta strandi481 – 49111
Helixi494 – 50916
Beta strandi513 – 5164
Beta strandi518 – 52710
Helixi528 – 5303
Helixi535 – 54612
Helixi554 – 56310
Helixi574 – 58714
Helixi589 – 5935
Turni597 – 5993
Beta strandi600 – 6023
Helixi606 – 6138

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi PH0853.
RefSeqi NP_418591.1. NC_000913.3.
YP_492312.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B62 X-ray 2.10 A 1-349 [» ]
1B63 X-ray 1.90 A 1-331 [» ]
1BKN X-ray 2.90 A/B 1-349 [» ]
1NHH X-ray 2.40 A 1-331 [» ]
1NHI X-ray 2.00 A 1-331 [» ]
1NHJ X-ray 2.30 A 1-331 [» ]
1X9Z X-ray 2.10 A/B 432-615 [» ]
ProteinModelPortali P23367.
SMRi P23367. Positions 1-331, 433-614.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10285N.
IntActi P23367. 12 interactions.
MINTi MINT-1266937.
STRINGi 511145.b4170.

Proteomic databases

PaxDbi P23367.
PRIDEi P23367.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77127 ; AAC77127 ; b4170 .
BAE78171 ; BAE78171 ; BAE78171 .
GeneIDi 12934482.
948691.
KEGGi ecj:Y75_p4056.
eco:b4170.
PATRICi 32123913. VBIEscCol129921_4301.

Organism-specific databases

EchoBASEi EB1258.
EcoGenei EG11281. mutL.

Phylogenomic databases

eggNOGi COG0323.
HOGENOMi HOG000256551.
InParanoidi P23367.
KOi K03572.
OMAi FSHIDEI.
OrthoDBi EOG6P8TMH.
PhylomeDBi P23367.

Enzyme and pathway databases

BioCyci EcoCyc:EG11281-MONOMER.
ECOL316407:JW4128-MONOMER.
MetaCyc:EG11281-MONOMER.

Miscellaneous databases

EvolutionaryTracei P23367.
PROi P23367.

Gene expression databases

Genevestigatori P23367.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
HAMAPi MF_00149. DNA_mis_repair.
InterProi IPR013507. 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 ]
PANTHERi PTHR10073:SF12. PTHR10073:SF12. 1 hit.
Pfami PF01119. DNA_mis_repair. 1 hit.
PF08676. MutL_C. 1 hit.
[Graphical view ]
SMARTi SM00387. HATPase_c. 1 hit.
SM00853. MutL_C. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
TIGRFAMsi TIGR00585. mutl. 1 hit.
PROSITEi PS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1992) [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(1995) [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(2006) [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(1991) [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(1994) [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(1998) [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(1999) [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: October 29, 2014
This is version 136 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