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MYCTU:O53896

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Species (Taxon ID) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). (83332)
Gene Name(s) pepD (ECO:0000313 with EMBL:CCP43733.1)
Protein Name(s) Peptidase S1 (ECO:0000313 with EMBL:AIR13718.1)

Probable serine protease PepD (Serine proteinase) (MTB32B) (ECO:0000313 with EMBL:CCP43733.1) Serine protease PepD (ECO:0000313 with EMBL:AFN48872.1)

External Links
UniProt O53896
EMBL CP003248
CP009480
AL123456
JLDD01000011
RefSeq NP_215498.1
YP_006514343.1
PDB 1Y8T
2Z9I
PDBsum 1Y8T
2Z9I
SMR O53896
STRING 83332.Rv0983
MEROPS S01.494
PRIDE O53896
EnsemblBacteria AFN48872
CCP43733
GeneID 13319543
885382
KEGG mtu:Rv0983
mtv:RVBD_0983
PATRIC 18150710
KO K08372
OMA TINDPRE
OrthoDB EOG6XQ3NR
PhylomeDB O53896
BioCyc MTBRV:RV0983-MONOMER
Proteomes UP000001584
UP000003123
GO GO:0005576
GO:0004252
GO:0008236
GO:0009405
GO:0030163
GO:0006508
GO:0006950
Gene3D 2.30.42.10
InterPro IPR001478
IPR001940
IPR009003
Pfam PF13180
PRINTS PR00834
SMART SM00228
SUPFAM SSF50156
SSF50494
PROSITE PS50106

Annotations

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

proteolysis

PMID:21445360[1]

ECO:0000314

P

Proteins that interact with PepD were selected by co-immunoprecipitation carried out with with M. smegmatis ΔpepD (Figure 2C). These were then identified using LC MS/MS, and co-immunoprecipitation and LC MS/MS were repeated with M. tuberculosis Δpep, indicating several proteins which interact with PepD (Tables S3-7).The 35-kDa antigen was the top scoring protein for probable interaction with PepD(Table 1). Specifically with the 35-kDa antigenFigure 3D shows the presence of a lower molecular weight protein that is immunoreactive with the anti-FLAG monoclonal antibody in the wild-type M. tuberculosis pepD strain. This indicates that PepD interacts with/ cleaves the 35-kDa antigen

complete

involved_in

GO:0030163

protein catabolic process

PMID:18479146[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009405

pathogenesis

PMID:18479146[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008236

serine-type peptidase activity

PMID:20061478[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008236

serine-type peptidase activity

PMID:18479146[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0071236

cellular response to antibiotic

PMID:20061478[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:20061478[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

PMID:21148733[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

PMID:10417166[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004252

serine-type endopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001940

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001940

P

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

Notes

References

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

  1. White, MJ et al. (2011) The HtrA-like serine protease PepD interacts with and modulates the Mycobacterium tuberculosis 35-kDa antigen outer envelope protein. PLoS ONE 6 e18175 PubMed GONUTS page
  2. 2.0 2.1 2.2 Mohamedmohaideen, NN et al. (2008) Structure and function of the virulence-associated high-temperature requirement A of Mycobacterium tuberculosis. Biochemistry 47 6092-102 PubMed GONUTS page
  3. 3.0 3.1 3.2 White, MJ et al. (2010) PepD participates in the mycobacterial stress response mediated through MprAB and SigE. J. Bacteriol. 192 1498-510 PubMed GONUTS page
  4. McCann, JR et al. (2011) Genome-wide identification of Mycobacterium tuberculosis exported proteins with roles in intracellular growth. J. Bacteriol. 193 854-61 PubMed GONUTS page
  5. Skeiky, YA et al. (1999) Cloning, expression, and immunological evaluation of two putative secreted serine protease antigens of Mycobacterium tuberculosis. Infect. Immun. 67 3998-4007 PubMed GONUTS page