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Description:
DNA mismatch repair protein mutL.
Molecular weight: 67924
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 ) mismatch repair( GO:0006298 )
Important dates:
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 2.
07-MAR-2006, entry version 58.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Escherichia.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein MUTL_ECOLI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | Z11831 | CAA77850.1 | - |
| EMBL | U14003 | AAA97066.1 | - |
| EMBL | U00096 | AAC77127.1 | - |
| EMBL | M63655 | AAA24173.1 | - |
| EMBL | L19346 | AAA20098.1 | - |
| PIR | PH0853 | PH0853. | |
| PDB | 1B62 | X-ray | A=1-349. |
| PDB | 1B63 | X-ray | A=1-331. |
| PDB | 1BKN | X-ray | A/B=1-349. |
| PDB | 1X9Z | X-ray | A/B=432-615. |
| IntAct | P23367 | -.1 | |
| GenomeReviews | U00096_GR | b4170.1 | |
| EchoBASE | EB1258 | -.1 | |
| EcoGene | EG11281 | mutL. | |
| BioCyc | EcoCyc:EG11281-MONOMER | -.1 | |
| GO | GO:0005515 | F:protein binding | IPI. |
| HAMAP | MF_00149 | - | 1. |
| InterPro | IPR003594 | ATP_bd_ATPase. | |
| InterPro | IPR002099 | DNA_mis_repair. | |
| PANTHER | PTHR10073 | DNA_mis_repair.1 | 1. |
| Pfam | PF01119 | DNA_mis_repair | 1. |
| Pfam | PF02518 | HATPase_c | 1. |
| TIGRFAMs | TIGR00585 | mutl | 1. |
| PROSITE | PS00058 | DNA_MISMATCH_REPAIR_1 | 1. |
Keywords:
3D-structure; ATP-binding; Complete proteome; DNA damage; DNA repair; Nucleotide-binding.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=92279041; PubMed=1594459;
RA Tsui H.-C.T., Mandavilli B.S., Winkler M.E.;
RT "Nonconserved segment of the MutL protein from Escherichia coli K-12
RT and Salmonella typhimurium.";
RL Nucleic Acids Res. 20:2379-2379(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=95334362; PubMed=7610040;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
RA Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the
RT region from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 596-615.
RC STRAIN=K12;
RX MEDLINE=91154127; PubMed=1999389;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RC STRAIN=K12;
RX MEDLINE=94195106; PubMed=7511774;
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
RT with a gene encoding a new cell-wall amidase.";
RL Mol. Microbiol. 11:189-202(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-349.
RX MEDLINE=99043508; 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
RT repair and mutagenesis.";
RL Cell 95:541-552(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-349.
RC STRAIN=K12;
RX MEDLINE=99213497; 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).
Feature:
CHAIN 1 615 DNA mismatch repair protein mutL.
/FTId=PRO_0000177943.
STRAND 1 1
STRAND 4 5
HELIX 8 19
STRAND 21 22
HELIX 23 36
TURN 37 38
STRAND 40 47
HELIX 48 50
TURN 51 51
STRAND 52 58
STRAND 60 60
HELIX 65 72
STRAND 73 73
TURN 74 75
STRAND 76 79
STRAND 82 82
HELIX 83 87
TURN 88 88
STRAND 91 92
STRAND 95 96
HELIX 98 103
TURN 104 105
STRAND 106 113
TURN 115 116
STRAND 118 126
TURN 127 130
STRAND 131 137
STRAND 141 149
TURN 150 153
HELIX 155 159
TURN 160 160
HELIX 164 181
TURN 183 184
STRAND 186 191
TURN 192 193
STRAND 194 199
TURN 204 205
TURN 208 208
HELIX 209 216
HELIX 218 223
STRAND 224 231
TURN 232 233
STRAND 234 241
HELIX 243 245
TURN 248 249
HELIX 250 252
STRAND 254 258
TURN 259 260
STRAND 261 262
HELIX 266 279
STRAND 280 282
STRAND 288 293
HELIX 296 298
STRAND 299 300
TURN 302 303
STRAND 304 304
TURN 305 306
STRAND 311 312
TURN 313 314
HELIX 315 329
TURN 330 330
STRAND 437 442
TURN 443 445
STRAND 446 451
TURN 452 453
STRAND 454 459
HELIX 460 472
STRAND 473 474
TURN 475 476
STRAND 477 477
STRAND 481 491
HELIX 494 509
TURN 510 511
STRAND 513 516
STRAND 518 527
HELIX 528 530
TURN 531 532
STRAND 533 533
HELIX 535 546
TURN 547 548
STRAND 550 551
HELIX 554 563
TURN 564 565
STRAND 566 566
STRAND 571 571
HELIX 574 587
HELIX 589 593
STRAND 594 594
TURN 597 599
STRAND 600 602
HELIX 606 613
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.
-!- INTERACTION:
P06722:mutH; NbExp=2; IntAct=EBI-554913, EBI-545170;
P03018:uvrD; NbExp=2; IntAct=EBI-554913, EBI-559573;
-!- SIMILARITY: Belongs to the DNA mismatch repair mutL/hexB family.
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Sequence length: 615
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