Difference between revisions of "PepT"
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| + | = [[Categories]] containing this gene/protein = | ||
| + | {{SubtiWiki category|[[utilization of nitrogen sources other than amino acids]]}} | ||
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| + | = This gene is a member of the following [[regulons]] = | ||
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=The gene= | =The gene= | ||
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=The protein= | =The protein= | ||
Revision as of 01:51, 9 December 2010
- Description: peptidase T (tripeptidase), zinc-dependent
| Gene name | pepT |
| Synonyms | |
| Essential | no |
| Product | peptidase T (tripeptidase) |
| Function | peptide degradation |
| MW, pI | 45 kDa, 4.538 |
| Gene length, protein length | 1230 bp, 410 aa |
| Immediate neighbours | yxjL, yxjJ |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
Categories containing this gene/protein
utilization of nitrogen sources other than amino acids
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU38920
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Release of the N-terminal residue from a tripeptide (according to Swiss-Prot)
- Protein family: peptidase M20B family (according to Swiss-Prot)
- Paralogous protein(s): YqjE
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure: 3GBO (from Bacillus cereus (71% identity), to be published)
- UniProt: P55179
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: pepT PubMed
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
M H Cha, W M Yong, S M Lee, Y S Lee, I Y Chung
The biochemical and molecular characterization of recombinant Bacillus subtilis tripeptidase (PepT) as a zinc-dependent metalloenzyme.
Mol Cells: 2000, 10(4);423-31
[PubMed:10987140]
[WorldCat.org]
(P p)
O Schrögel, O Krispin, R Allmansberger
Expression of a pepT homologue from Bacillus subtilis.
FEMS Microbiol Lett: 1996, 145(3);341-8
[PubMed:8978088]
[WorldCat.org]
[DOI]
(P p)
