DNA mismatch repair protein MutL - Escherichia coli (strain K12)

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P23367 (MUTL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 124. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
DNA mismatch repair protein MutL

Gene names

Name:	mutL
Ordered Locus Names:	b4170, JW4128

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	615 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00149

Sequence similarities

Belongs to the DNA mismatch repair MutL/HexB family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Ligand	ATP-binding Nucleotide-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mismatch repair Inferred from direct assay PubMed 2665076. Source: EcoliWiki regulation of DNA recombination Inferred from mutant phenotype PubMed 2555716. Source: EcoliWiki
Cellular_component	mismatch repair complex Inferred from genetic interaction PubMed 6987663. Source: EcoliWiki
Molecular_function	ATP binding Inferred from direct assay PubMed 12606120 Ref.7. Source: EcoliWiki ATPase activity Inferred from direct assay Ref.7. Source: EcoliWiki mismatched DNA binding Inferred from electronic annotation. Source: InterPro single-stranded DNA binding Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
holA	P28630	2	EBI-554913,EBI-549153
holB	P28631	2	EBI-554913,EBI-549161
mutH	P06722	8	EBI-554913,EBI-545170
recA	P0A7G6	3	EBI-554913,EBI-370331
uvrD	P03018	7	EBI-554913,EBI-559573
vsr	P09184	3	EBI-554913,EBI-765033

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 615

615

DNA mismatch repair protein MutL HAMAP-Rule MF_00149

PRO_0000177943

Secondary structure

615

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P23367 [UniParc].

Last modified May 1, 1992. Version 2.
Checksum: C69D2735BF5FA165
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FASTA

615

67,924

        10         20         30         40         50         60 
MPIQVLPPQL ANQIAAGEVV ERPASVVKEL VENSLDAGAT RIDIDIERGG AKLIRIRDNG 

        70         80         90        100        110        120 
CGIKKDELAL ALARHATSKI ASLDDLEAII SLGFRGEALA SISSVSRLTL TSRTAEQQEA 

       130        140        150        160        170        180 
WQAYAEGRDM NVTVKPAAHP VGTTLEVLDL FYNTPARRKF LRTEKTEFNH IDEIIRRIAL 

       190        200        210        220        230        240 
ARFDVTINLS HNGKIVRQYR AVPEGGQKER RLGAICGTAF LEQALAIEWQ HGDLTLRGWV 

       250        260        270        280        290        300 
ADPNHTTPAL AEIQYCYVNG RMMRDRLINH AIRQACEDKL GADQQPAFVL YLEIDPHQVD 

       310        320        330        340        350        360 
VNVHPAKHEV RFHQSRLVHD FIYQGVLSVL QQQLETPLPL DDEPQPAPRS IPENRVAAGR 

       370        380        390        400        410        420 
NHFAEPAARE PVAPRYTPAP ASGSRPAAPW PNAQPGYQKQ QGEVYRQLLQ TPAPMQKLKA 

       430        440        450        460        470        480 
PEPQEPALAA NSQSFGRVLT IVHSDCALLE RDGNISLLSL PVAERWLRQA QLTPGEAPVC 

       490        500        510        520        530        540 
AQPLLIPLRL KVSAEEKSAL EKAQSALAEL GIDFQSDAQH VTIRAVPLPL RQQNLQILIP 

       550        560        570        580        590        600 
ELIGYLAKQS VFEPGNIAQW IARNLMSEHA QWSMAQAITL LADVERLCPQ LVKTPPGGLL 

       610 
QSVDLHPAIK ALKDE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

PH0853.

RefSeq

NP_418591.1. NC_000913.2.
YP_492312.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P23367.

SMR

P23367. Positions 1-331, 433-614.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10285N.

IntAct

P23367. 12 interactions.

MINT

MINT-1266937.

STRING

511145.b4170.

Proteomic databases

PaxDb

P23367.

PRIDE

P23367.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77127; AAC77127; b4170.
BAE78171; BAE78171; BAE78171.

GeneID

12934482.
948691.

KEGG

ecj:Y75_p4056.
eco:b4170.

PATRIC

32123913. VBIEscCol129921_4301.

Organism-specific databases

EchoBASE

EB1258.

EcoGene

EG11281. mutL.

Phylogenomic databases

eggNOG

COG0323.

HOGENOM

HOG000256551.

K03572.

OMA

FSHIDEI.

ProtClustDB

PRK00095.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P23367.

Family and domain databases

Gene3D

3.30.230.10. 1 hit.
3.30.565.10. 1 hit.

HAMAP

MF_00149. DNA_mis_repair.

InterPro

IPR002099. DNA_mismatch_repair.
IPR013507. DNA_mismatch_repair_C.
IPR014762. DNA_mismatch_repair_CS.
IPR020667. DNA_mismatch_repair_MutL.
IPR014763. DNA_mismatch_repair_N.
IPR003594. HATPase_ATP-bd.
IPR014790. MutL_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]

PANTHER

PTHR10073. PTHR10073. 1 hit.

Pfam

PF01119. DNA_mis_repair. 1 hit.
PF08676. MutL_C. 1 hit.
[Graphical view]

SMART

SM00387. HATPase_c. 1 hit.
SM00853. MutL_C. 1 hit.
[Graphical view]

SUPFAM

SSF55874. ATP_bd_ATPase. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.

TIGRFAMs

TIGR00585. mutl. 1 hit.

PROSITE

PS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P23367.

Entry information

Entry name

MUTL_ECOLI

Accession

Primary (citable) accession number: P23367
Secondary accession number(s): Q2M6D5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	May 1, 1992
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents