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ECOLI:UVRA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) uvrA (ECO:0000255 with HAMAP-Rule:MF_00205) (synonyms: dinE)
Protein Name(s) UvrABC system protein A (ECO:0000255 with HAMAP-Rule:MF_00205)

UvrA protein (ECO:0000255 with HAMAP-Rule:MF_00205) Excinuclease ABC subunit A (ECO:0000255 with HAMAP-Rule:MF_00205)

External Links
UniProt P0A698
EMBL M13495
U00006
U00096
AP009048
X01621
J01721
PIR A23869
RefSeq NP_418482.1
YP_492201.1
PDB 4DFC
PDBsum 4DFC
ProteinModelPortal P0A698
SMR P0A698
BioGrid 852853
DIP DIP-35876N
IntAct P0A698
MINT MINT-1257037
STRING 511145.b4058
PaxDb P0A698
PRIDE P0A698
EnsemblBacteria AAC77028
BAE78060
GeneID 12933676
948559
KEGG ecj:Y75_p3945
eco:b4058
PATRIC 32123661
EchoBASE EB1054
EcoGene EG11061
eggNOG COG0178
HOGENOM HOG000050448
InParanoid P0A698
KO K03701
OMA VIEMNFL
OrthoDB EOG6QK4PS
PhylomeDB P0A698
BioCyc EcoCyc:EG11061-MONOMER
ECOL316407:JW4019-MONOMER
MetaCyc:EG11061-MONOMER
PRO PR:P0A698
Proteomes UP000000318
UP000000625
Genevestigator P0A698
GO GO:0005737
GO:0009380
GO:0005524
GO:0016887
GO:0003677
GO:0009381
GO:0008270
GO:0006200
GO:0006281
GO:0006289
GO:0009432
Gene3D 3.30.1490.20
3.40.50.300
HAMAP MF_00205
InterPro IPR003439
IPR017871
IPR013815
IPR027417
IPR004602
Pfam PF00005
SUPFAM SSF52540
TIGRFAMs TIGR00630
PROSITE PS00211
PS50893

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0008094

DNA-dependent ATPase activity

PMID:2525700[1]

ECO:0000314

F

Figure 1 shows that the amount of ATP hydrolized by uvrA is dependent on the concentration of DNA

complete

GO:0032508

DNA duplex unwinding

PMID:3024109[2]

ECO:0000314

P

Figure 2 shows that uvrA will unwind dsDNA in the presence of nucleotides such as ATP-γ-S

complete

GO:0006281

DNA repair

PMID:3024109[2]

ECO:0000314

P

Figure 5 shows that unwinding of DNA by uvrA increases with the number of dimers formed from UV damage in the presence of ATP

complete

part_of

GO:0009380

excinuclease repair complex

PMID:12145219[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:2546148[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A698

F

Seeded From UniProt

complete

enables

GO:0016887

ATPase activity

PMID:19208636[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009314

response to radiation

PMID:27718375[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006281

DNA repair

PMID:2690930[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:17309111[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

PMID:19208636[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0090305

nucleic acid phosphodiester bond hydrolysis

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004518

P

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004602

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003439
InterPro:IPR017871

F

Seeded From UniProt

complete

involved_in

GO:0006289

nucleotide-excision repair

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004602

P

Seeded From UniProt

complete

part_of

GO:0009380

excinuclease repair complex

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004602

C

Seeded From UniProt

complete

enables

GO:0016887

ATPase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003439
InterPro:IPR004602
InterPro:IPR017871

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101266

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101266

F

Seeded From UniProt

complete

enables

GO:0009381

excinuclease ABC activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101266

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101266

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101266

C

Seeded From UniProt

complete

involved_in

GO:0009432

SOS response

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101266

P

Seeded From UniProt

complete

involved_in

GO:0006281

DNA repair

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101266

P

Seeded From UniProt

complete

involved_in

GO:0006289

nucleotide-excision repair

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000101266

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0227

P

Seeded From UniProt

complete

involved_in

GO:0006281

DNA repair

GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0228
UniProtKB-KW:KW-0234

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0009432

SOS response

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0742

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0004518

nuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0267

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ Oh, EY et al. (1989) ATPase activity of the UvrA and UvrAB protein complexes of the Escherichia coli UvrABC endonuclease. Nucleic Acids Res. 17 4145-59 PubMed GONUTS page
  2. ↑ 2.0 2.1 Oh, EY & Grossman, L (1986) The effect of Escherichia coli Uvr protein binding on the topology of supercoiled DNA. Nucleic Acids Res. 14 8557-71 PubMed GONUTS page
  3. ↑ Verhoeven, EE et al. (2002) The presence of two UvrB subunits in the UvrAB complex ensures damage detection in both DNA strands. EMBO J. 21 4196-205 PubMed GONUTS page
  4. ↑ Orren, DK & Sancar, A (1989) The (A)BC excinuclease of Escherichia coli has only the UvrB and UvrC subunits in the incision complex. Proc. Natl. Acad. Sci. U.S.A. 86 5237-41 PubMed GONUTS page
  5. ↑ 5.0 5.1 Wagner, K et al. (2009) Single-molecule analysis reveals two separate DNA-binding domains in the Escherichia coli UvrA dimer. Nucleic Acids Res. 37 1962-72 PubMed GONUTS page
  6. ↑ Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page
  7. ↑ Lin, JJ & Sancar, A (1989) A new mechanism for repairing oxidative damage to DNA: (A)BC excinuclease removes AP sites and thymine glycols from DNA. Biochemistry 28 7979-84 PubMed GONUTS page
  8. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  9. ↑ Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page
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