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ECOLI:EX1

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) sbcB (synonyms: cpeA, xonA)
Protein Name(s) Exodeoxyribonuclease I

ExoI (ECO:0000303 with PMID:11101894[1]) Exonuclease I (ECO:0000303 with PMID:11101894[1]) DNA deoxyribophosphodiesterase dRPase

External Links
UniProt P04995
EMBL J02641
U00009
U00096
AP009048
PIR B64966
RefSeq NP_416515.1
PDB 1FXX
2QXF
3C94
3C95
3HL8
3HP9
4HCB
4HCC
4JRP
4JRQ
4JS4
4JS5
PDBsum 1FXX
2QXF
3C94
3C95
3HL8
3HP9
4HCB
4HCC
4JRP
4JRQ
4JS4
4JS5
ProteinModelPortal P04995
SMR P04995
DIP DIP-10827N
IntAct P04995
MINT MINT-1241098
STRING 511145.b2011
PaxDb P04995
PRIDE P04995
EnsemblBacteria AAC75072
BAA15839
GeneID 946529
KEGG eco:b2011
PATRIC 32119357
EchoBASE EB0919
EcoGene EG10926
eggNOG COG2925
HOGENOM HOG000276591
InParanoid P04995
KO K01141
OMA RDRPAQF
OrthoDB EOG6MWN7F
PhylomeDB P04995
BioCyc EcoCyc:EG10926-MONOMER
ECOL316407:JW1993-MONOMER
MetaCyc:EG10926-MONOMER
BRENDA 3.1.11.1
EvolutionaryTrace P04995
PRO PR:P04995
Proteomes UP000000318
UP000000625
GO GO:0000175
GO:0008852
GO:0000287
GO:0003697
GO:0006308
GO:0006281
GO:0090305
GO:0090503
Gene3D 3.30.420.10
InterPro IPR023607
IPR013620
IPR013520
IPR012337
Pfam PF08411
PF00929
PIRSF PIRSF000977
SUPFAM SSF53098

Annotations

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

involved_in

GO:0000738

DNA catabolic process, exonucleolytic

PMID:23609540[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

GO:0000175

3'-5'-exoribonuclease activity

PMID:4927675[3]

ECO:0000315

F

As shown in Table 3, the wildtype strain of the gene sbcB shows exonuclease activity. When the anitserum, that inhibits exonuclease activity, was added the exonuclease activity decreased proving the exonuclease activity of the crude lysates. To verify the sbcB gene activity, the gene was mutated, sbcB15 and when mutated the exonuclease activity decreased to show that the sbcB gene is responsible for exonuclease activity.

complete
CACAO 11104

involved_in

GO:0000738

DNA catabolic process, exonucleolytic

PMID:20018747[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000738

DNA catabolic process, exonucleolytic

PMID:18591666[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0051575

5'-deoxyribose-5-phosphate lyase activity

PMID:1329027[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003697

single-stranded DNA binding

PMID:23609540[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:23609540[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:20018747[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:18591666[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:11101894[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:18219121[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008310

single-stranded DNA 3'-5' exodeoxyribonuclease activity

PMID:23609540[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008310

single-stranded DNA 3'-5' exodeoxyribonuclease activity

PMID:20018747[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008310

single-stranded DNA 3'-5' exodeoxyribonuclease activity

PMID:18591666[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000175

3'-5'-exoribonuclease activity

PMID:21873635[8]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12480
PANTHER:PTN000114086
SGD:S000004049

F

Seeded From UniProt

complete

enables

GO:0008852

exodeoxyribonuclease I activity

PMID:14235546[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006308

DNA catabolic process

PMID:14235546[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0090503

RNA phosphodiester bond hydrolysis, exonucleolytic

GO_REF:0000108

ECO:0000364

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

GO:0000175

P

Seeded From UniProt

complete

enables

GO:0003676

nucleic acid binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR036397

F

Seeded From UniProt

complete

enables

GO:0004529

exodeoxyribonuclease activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR023607

F

Seeded From UniProt

complete

involved_in

GO:0006281

DNA repair

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013620

P

Seeded From UniProt

complete

enables

GO:0008852

exodeoxyribonuclease I activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013620

F

Seeded From UniProt

complete

enables

GO:0008852

exodeoxyribonuclease I activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.11.1

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

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

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

enables

GO:0004527

exonuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0269

F

Seeded From UniProt

complete

involved_in

GO:0006281

DNA repair

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0234

P

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-0540

F

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

edit table

Notes

References

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

  1. ↑ 1.0 1.1 1.2 Breyer, WA & Matthews, BW (2000) Structure of Escherichia coli exonuclease I suggests how processivity is achieved. Nat. Struct. Biol. 7 1125-8 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 2.3 Korada, SK et al. (2013) Crystal structures of Escherichia coli exonuclease I in complex with single-stranded DNA provide insights into the mechanism of processive digestion. Nucleic Acids Res. 41 5887-97 PubMed GONUTS page
  3. ↑ Kushner, SR et al. (1971) Genetic recombination in Escherichia coli: the role of exonuclease I. Proc. Natl. Acad. Sci. U.S.A. 68 824-7 PubMed GONUTS page
  4. ↑ 4.0 4.1 4.2 Lu, D et al. (2010) Small-molecule tools for dissecting the roles of SSB/protein interactions in genome maintenance. Proc. Natl. Acad. Sci. U.S.A. 107 633-8 PubMed GONUTS page
  5. ↑ 5.0 5.1 5.2 Lu, D & Keck, JL (2008) Structural basis of Escherichia coli single-stranded DNA-binding protein stimulation of exonuclease I. Proc. Natl. Acad. Sci. U.S.A. 105 9169-74 PubMed GONUTS page
  6. ↑ Sandigursky, M & Franklin, WA (1992) DNA deoxyribophosphodiesterase of Escherichia coli is associated with exonuclease I. Nucleic Acids Res. 20 4699-703 PubMed GONUTS page
  7. ↑ Busam, RD (2008) Structure of Escherichia coli exonuclease I in complex with thymidine 5'-monophosphate. Acta Crystallogr. D Biol. Crystallogr. 64 206-10 PubMed GONUTS page
  8. ↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  9. ↑ 9.0 9.1 LEHMAN, IR & NUSSBAUM, AL (1964) THE DEOXYRIBONUCLEASES OF ESCHERICHIA COLI. V. ON THE SPECIFICITY OF EXONUCLEASE I (PHOSPHODIESTERASE). J. Biol. Chem. 239 2628-36 PubMed GONUTS page
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