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ECOLI:YOEB

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) yoeB
Protein Name(s) Toxin YoeB

Putative endoribonuclease YoeB Putative mRNA interferase Yoeb

External Links
UniProt P69348
EMBL U00096
AP009048
RefSeq YP_490259.1
YP_588458.1
PDB 2A6Q
2A6R
2A6S
PDBsum 2A6Q
2A6R
2A6S
ProteinModelPortal P69348
SMR P69348
IntAct P69348
STRING 511145.b4539
EnsemblBacteria ABD18681
BAE76569
GeneID 12931408
1450274
KEGG ecj:Y75_p1979
eco:b4539
PATRIC 32119369
EchoBASE EB4102
EcoGene EG14356
eggNOG COG4115
HOGENOM HOG000216470
InParanoid P69348
KO K01175
OMA GEHRLVY
OrthoDB EOG6KWZ5K
PhylomeDB P69348
BioCyc EcoCyc:MONOMER0-1041
ECOL316407:JW5331-MONOMER
MetaCyc:MONOMER0-1041
EvolutionaryTrace P69348
PRO PR:P69348
Proteomes UP000000318
UP000000625
Genevestigator P69348
GO GO:0004521
GO:0016892
GO:0043024
GO:0003723
GO:0003714
GO:0006402
GO:0006379
GO:1903507
GO:0045947
GO:0006355
GO:0090502
GO:0044010
GO:0006351
InterPro IPR009614
Pfam PF06769
TIGRFAMs TIGR02116

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0008428

ribonuclease inhibitor activity

PMID:19141481[1]

ECO:0000269

F

Figure 1 shows the down-regulation of RNase III activity by YmdB.

complete
CACAO 3195

involved_in

GO:0098795

mRNA cleavage involved in gene silencing

PMID:15009896[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045947

negative regulation of translational initiation

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG14356
PANTHER:PTN002210985

P

Seeded From UniProt

complete

enables

GO:0043024

ribosomal small subunit binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG14356
PANTHER:PTN002210985

F

Seeded From UniProt

complete

enables

GO:0016892

endoribonuclease activity, producing 3'-phosphomonoesters

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG14356
PANTHER:PTN002210985

F

Seeded From UniProt

complete

involved_in

GO:0006401

RNA catabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002210985
UniProtKB:P9WF09

P

Seeded From UniProt

complete

enables

GO:0003714

transcription corepressor activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG14356
PANTHER:PTN002210985

F

Seeded From UniProt

complete

involved_in

GO:0045947

negative regulation of translational initiation

PMID:19124462[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0044010

single-species biofilm formation

PMID:19060153[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0043024

ribosomal small subunit binding

PMID:19124462[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016892

endoribonuclease activity, producing 3'-phosphomonoesters

PMID:23945936[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006402

mRNA catabolic process

PMID:18854355[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004521

endoribonuclease activity

PMID:16109374[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0090502

RNA phosphodiester bond hydrolysis, endonucleolytic

GO_REF:0000108

ECO:0000364

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

GO:0004521

P

Seeded From UniProt

complete

involved_in

GO:0090502

RNA phosphodiester bond hydrolysis, endonucleolytic

GO_REF:0000108

ECO:0000364

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

GO:0016892

P

Seeded From UniProt

complete

involved_in

GO:0090502

RNA phosphodiester bond hydrolysis, endonucleolytic

GO_REF:0000108

ECO:0000364

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

GO:0016892

P

Seeded From UniProt

complete

involved_in

GO:1903507

negative regulation of nucleic acid-templated transcription

GO_REF:0000108

ECO:0000364

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

GO:0003714

P

Seeded From UniProt

complete

enables

GO:0004519

endonuclease activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR009614

F

Seeded From UniProt

complete

involved_in

GO:0006401

RNA catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR009614

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:0003723

RNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0694

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

enables

GO:0004519

endonuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0255

F

Seeded From UniProt

complete

Notes

References

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

  1. Kim, KS et al. (2008) YmdB: a stress-responsive ribonuclease-binding regulator of E. coli RNase III activity. Genes Dev. 22 3497-508 PubMed GONUTS page
  2. Christensen, SK et al. (2004) Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: involvement of the yefM-yoeB toxin-antitoxin system. Mol. Microbiol. 51 1705-17 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. 4.0 4.1 Zhang, Y & Inouye, M (2009) The inhibitory mechanism of protein synthesis by YoeB, an Escherichia coli toxin. J. Biol. Chem. 284 6627-38 PubMed GONUTS page
  5. Kim, Y et al. (2009) Toxin-antitoxin systems in Escherichia coli influence biofilm formation through YjgK (TabA) and fimbriae. J. Bacteriol. 191 1258-67 PubMed GONUTS page
  6. Feng, S et al. (2013) YoeB-ribosome structure: a canonical RNase that requires the ribosome for its specific activity. Nucleic Acids Res. 41 9549-56 PubMed GONUTS page
  7. Christensen-Dalsgaard, M & Gerdes, K (2008) Translation affects YoeB and MazF messenger RNA interferase activities by different mechanisms. Nucleic Acids Res. 36 6472-81 PubMed GONUTS page
  8. Kamada, K & Hanaoka, F (2005) Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin. Mol. Cell 19 497-509 PubMed GONUTS page