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BACAN:LEF

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Species (Taxon ID) Bacillus anthracis. (1392)
Gene Name(s) lef
Protein Name(s) Lethal factor

LF Anthrax lethal toxin endopeptidase component

External Links
UniProt P15917
EMBL M29081
M30210
AF065404
AE011190
AE017336
AJ413934
AJ413935
PIR JQ0032
RefSeq NP_052803.1
NP_652928.1
WP_010890024.1
YP_016503.2
PDB 1J7N
1JKY
1PWP
1PWQ
1PWU
1PWV
1PWW
1YQY
1ZXV
2L0R
3KWV
4DV8
4PKQ
4PKR
4PKS
4PKT
4PKU
4PKV
4PKW
PDBsum 1J7N
1JKY
1PWP
1PWQ
1PWU
1PWV
1PWW
1YQY
1ZXV
2L0R
3KWV
4DV8
4PKQ
4PKR
4PKS
4PKT
4PKU
4PKV
4PKW
ProteinModelPortal P15917
SMR P15917
DIP DIP-29871N
IntAct P15917
MINT MINT-7014731
STRING 261594.GBAA_pXO1_0172
BindingDB P15917
ChEMBL CHEMBL4372
MEROPS M34.001
EnsemblBacteria AAT28913
GeneID 1158731
2820148
3361711
KEGG bar:GBAA_pXO1_0172
PATRIC 24662141
eggNOG NOG45846
HOGENOM HOG000034565
KO K08645
OMA RMMARYE
OrthoDB EOG62ZHV6
BioCyc ANTHRA:GBAA_PXO1_0172-MONOMER
BANT261594:GJ7F-5757-MONOMER
Reactome REACT_228255
EvolutionaryTrace P15917
Proteomes UP000000594
GO GO:0005576
GO:0046872
GO:0008237
GO:0009405
GO:0006508
Gene3D 1.10.2030.10
3.40.390.10
InterPro IPR015239
IPR003541
IPR014781
IPR024079
Pfam PF09156
PF07737
PRINTS PR01392
PROSITE PS00142

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0006508

proteolysis

PMID:22438953[1]

ECO:0000314

P

figure 5 demonstrated that "the specific proteolytic activity of lethal factor of the MKKs is required for the anti-proliferate and pro-apoptotic effects of lethal toxin on the intestinal epithelium" ; the data also established the proteolysis activity of lethal factor of Anthrax lethal toxin

complete
CACAO 4088

GO:0006508

proteolysis

PMID:24478317[2]

ECO:0000314

P

Figure 9.

complete
CACAO 9632

GO:0009405

pathogenesis

PMID:22438953[1]

ECO:0000270

P

figure 2 - "in time course study, lethal toxin-induced pathological changes became evident in the intestine 48 hours post lethal toxin exposure. these changes included the onset of villous damage and minor hemorrhage. by 72 hours post lethal toxin exposure, focal areas showed marked destruction of the normal villous structures, accompanied by ares ulceration"

complete
CACAO 4090

GO:0006508

proteolysis

PMID:23152930[3]

ECO:0000314

P

Figure 2 and 3

complete
CACAO 6047

GO:0008237

metallopeptidase activity

PMID:7854123[4]

ECO:0000247

UniProtKB:P04958


F

Figure 1. Shows DNA sequence comparison of LEF with other proteins from different organisms that present metallopeptidase activity. Lethal factor sequence contain the HEXXH motif inferring its metallopeptidase activity

complete
CACAO 11021

GO:0008270

zinc ion binding

PMID:7854123[4]

ECO:0000314

F

Figure 3. Shows LEF binding to radioactive labeled zinc binding

complete
CACAO 11022

involved_in

GO:0010629

negative regulation of gene expression

PMID:23626836[5]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P13423

P

  • has_regulation_target:(UniProtKB:O54942)
  • occurs_in:(CL:0002262)
  • occurs_in:(UBERON:0002107)

Seeded From UniProt

complete

involved_in

GO:0061136

regulation of proteasomal protein catabolic process

PMID:23626836[5]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P13423

P

Seeded From UniProt

complete

involved_in

GO:0001933

negative regulation of protein phosphorylation

PMID:23626836[5]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P13423

P

Seeded From UniProt

complete

involved_in

GO:0043409

negative regulation of MAPK cascade

PMID:23626836[5]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P13423

P

occurs_in:(CL:2000016)

Seeded From UniProt

complete

involved_in

GO:0035897

proteolysis in other organism

PMID:23626836[5]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P13423

P

Seeded From UniProt

complete

NOT|involved_in

GO:0097300

programmed necrotic cell death

PMID:23626836[5]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P13423

P

Seeded From UniProt

complete

involved_in

GO:0044533

positive regulation of apoptotic process in other organism

PMID:23626836[5]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P13423

P

occurs_in:(CL:2000016)

Seeded From UniProt

complete

involved_in

GO:0000122

negative regulation of transcription by RNA polymerase II

PMID:23626836[5]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P13423

P

Seeded From UniProt

complete

NOT|involved_in

GO:1903140

regulation of establishment of endothelial barrier

PMID:23626836[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1903140

regulation of establishment of endothelial barrier

PMID:23626836[5]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P13423

P

Seeded From UniProt

complete

involved_in

GO:0009405

pathogenesis

PMID:22438953[1]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:23152930[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003541

F

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003541

C

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR024079

F

Seeded From UniProt

complete

involved_in

GO:0009405

pathogenesis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003541

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003541

F

Seeded From UniProt

complete

involved_in

GO:0035897

proteolysis in other organism

Reactome:R-HSA-5211405
Reactome:R-HSA-5211400
Reactome:R-HSA-5211391
Reactome:R-HSA-5211387
Reactome:R-HSA-5211356
Reactome:R-HSA-5211340

ECO:0000304

author statement supported by traceable reference used in manual assertion






P

Seeded From UniProt

complete

involved_in

GO:0009405

pathogenesis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0843

P

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0964
UniProtKB-SubCell:SL-0243

C

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:0090729

toxin activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0800

F

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0482

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

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

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 Sun, C et al. (2012) Anthrax lethal toxin disrupts intestinal barrier function and causes systemic infections with enteric bacteria. PLoS ONE 7 e33583 PubMed GONUTS page
  2. ↑ Rivera, J et al. (2014) Platelet-activating factor contributes to Bacillus anthracis lethal toxin-associated damage. J. Biol. Chem. 289 7131-41 PubMed GONUTS page
  3. ↑ 3.0 3.1 Hellmich, KA et al. (2012) Anthrax lethal factor cleaves mouse nlrp1b in both toxin-sensitive and toxin-resistant macrophages. PLoS ONE 7 e49741 PubMed GONUTS page
  4. ↑ 4.0 4.1 Klimpel, KR et al. (1994) Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity. Mol. Microbiol. 13 1093-100 PubMed GONUTS page
  5. ↑ 5.0 5.1 5.2 5.3 5.4 5.5 5.6 5.7 5.8 5.9 D'Agnillo, F et al. (2013) Anthrax lethal toxin downregulates claudin-5 expression in human endothelial tight junctions. PLoS ONE 8 e62576 PubMed GONUTS page
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