Reviewed, UniProtKB/Swiss-Prot P23367 (MUTL_ECOLI)

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) [Complete 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 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
Gene Ontology (GO)
Biological process	mismatch repair Inferred from direct assay. Source: UniProtKB
Cellular component	mismatch repair complex Inferred from genetic interaction. Source: UniProtKB
Molecular function	ATP binding Ref.7 Inferred from direct assay. Source: UniProtKB ATPase activity Ref.7 Inferred from direct assay. Source: UniProtKB mismatched DNA binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
mutH	P06722	2	EBI-554913,EBI-545170
tufA	P0A6N1	1	EBI-554913,EBI-301077
uvrD	P03018	2	EBI-554913,EBI-559573

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 MF_00149

PRO_0000177943

Secondary structure

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615

Helix Strand Turn

Details...

Helix

8 – 19

12

Helix

23 – 36

14

Beta strand

40 – 47

8

Turn

48 – 51

4

Beta strand

52 – 58

7

Helix

65 – 67

3

Helix

68 – 71

4

Beta strand

76 – 79

4

Helix

83 – 87

5

Helix

98 – 104

7

Beta strand

106 – 113

8

Beta strand

118 – 126

9

Turn

127 – 130

4

Beta strand

131 – 137

7

Beta strand

141 – 149

9

Turn

150 – 153

4

Helix

155 – 158

4

Helix

164 – 181

18

Beta strand

185 – 191

7

Beta strand

194 – 199

6

Helix

209 – 216

8

Helix

218 – 223

6

Beta strand

224 – 231

8

Beta strand

234 – 241

8

Helix

243 – 245

3

Helix

250 – 252

3

Beta strand

254 – 258

5

Beta strand

261 – 263

3

Helix

266 – 279

14

Beta strand

280 – 282

3

Beta strand

288 – 293

6

Helix

296 – 298

3

Helix

315 – 329

15

Beta strand

437 – 442

6

Turn

443 – 445

3

Beta strand

446 – 451

6

Beta strand

454 – 459

6

Helix

460 – 472

13

Beta strand

481 – 491

11

Helix

494 – 509

16

Beta strand

513 – 516

4

Beta strand

518 – 527

10

Helix

528 – 530

3

Helix

535 – 546

12

Helix

554 – 563

10

Helix

574 – 587

14

Helix

589 – 593

5

Turn

597 – 599

3

Beta strand

600 – 602

3

Helix

606 – 613

8

Sequences

	Sequence		Length	Mass (Da)
	P23367-1 [UniParc]. Last modified May 1, 1992. Version 2. Checksum: C69D2735BF5FA165	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

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: 1594459] [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: 7610040] [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: 9278503] [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: 16738553] [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: 1999389] [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: 7511774] [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: 9827806] [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: 10199405] [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

AP_004670.1.
NP_418591.1.

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10285N.

IntAct

P23367. 9 interactions.

STRING

P23367.

Genome annotation databases

GeneID

948691.

GenomeReviews

Gene locus JW4128 in contig AP009048_GR.
Gene locus b4170 in contig U00096_GR.

KEGG

ecj:JW4128.
eco:b4170.

Organism-specific databases

EchoBASE

EB1258.

EcoGene

EG11281. mutL.

CMR

Search...

Phylogenomic databases

eggNOG

COG0323.

HOGENOM

HBG520262.

OMA

FSHIDEI.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11281-MONOMER.
ECOL168927:B4170-MONOMER.
MetaCyc:EG11281-MONOMER.

Gene expression databases

Genevestigator

P23367.

Family and domain databases

HAMAP

MF_00149. DNA_mis_repair.
[Tree]

InterPro

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

Gene3D

G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.

PANTHER

PTHR10073. DNA_mis_repair. 1 hit.

Pfam

PF01119. DNA_mis_repair. 1 hit.
PF02518. HATPase_c. 1 hit.
PF08676. MutL_C. 1 hit.
[Graphical view]

SMART

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

TIGRFAMs

TIGR00585. mutl. 1 hit.

PROSITE

PS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	February 9, 2010
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)