Difference between revisions of "SipT"
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=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' | + | * '''Operon:''' ''sipT'' {{PubMed|9694797}} |
* '''[[Sigma factor]]:''' | * '''[[Sigma factor]]:''' | ||
| Line 95: | Line 95: | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| + | ** [[DegU]]: transcription activation {{PubMed|9694797}} | ||
* '''Additional information:''' | * '''Additional information:''' | ||
Revision as of 19:32, 8 October 2009
- Description: signal peptidase I
| Gene name | sipT |
| Synonyms | |
| Essential | no |
| Product | signal peptidase I |
| Function | protein secretion |
| MW, pI | 21 kDa, 9.851 |
| Gene length, protein length | 579 bp, 193 aa |
| Immediate neighbours | fruA, ykoA |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
The gene
Basic information
- Locus tag: BSU14410
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins (according to Swiss-Prot)
- Protein family: peptidase S26 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure:
- UniProt: P71013
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: sipT PubMed
- Regulation:
- 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
Tiina Pummi, Soile Leskelä, Eva Wahlström, Ulf Gerth, Harold Tjalsma, Michael Hecker, Matti Sarvas, Vesa P Kontinen
ClpXP protease regulates the signal peptide cleavage of secretory preproteins in Bacillus subtilis with a mechanism distinct from that of the Ecs ABC transporter.
J Bacteriol: 2002, 184(4);1010-8
[PubMed:11807061]
[WorldCat.org]
[DOI]
(P p)
H Tjalsma, A Bolhuis, M L van Roosmalen, T Wiegert, W Schumann, C P Broekhuizen, W J Quax, G Venema, S Bron, J M van Dijl
Functional analysis of the secretory precursor processing machinery of Bacillus subtilis: identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases.
Genes Dev: 1998, 12(15);2318-31
[PubMed:9694797]
[WorldCat.org]
[DOI]
(P p)
H Tjalsma, M A Noback, S Bron, G Venema, K Yamane, J M van Dijl
Bacillus subtilis contains four closely related type I signal peptidases with overlapping substrate specificities. Constitutive and temporally controlled expression of different sip genes.
J Biol Chem: 1997, 272(41);25983-92
[PubMed:9325333]
[WorldCat.org]
[DOI]
(P p)
