Difference between revisions of "SipT"
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|style="background:#ABCDEF;" align="center"|'''Function''' || protein secretion | |style="background:#ABCDEF;" align="center"|'''Function''' || protein secretion | ||
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| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU14410 sipT] |
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/wiki/index.php/Protein_secretion Protein secretion]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/wiki/index.php/Protein_secretion Protein secretion]''' | ||
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[fruA]]'', ''[[ykoA]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[fruA]]'', ''[[ykoA]]'' | ||
|- | |- | ||
| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU14410 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU14410 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU14410 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:sipT_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:sipT_context.gif]] | ||
Revision as of 12:43, 13 May 2013
- Description: signal peptidase I
| Gene name | sipT |
| Synonyms | |
| Essential | no |
| Product | signal peptidase I |
| Function | protein secretion |
| Gene expression levels in SubtiExpress: sipT | |
| Metabolic function and regulation of this protein in SubtiPathways: Protein secretion | |
| MW, pI | 21 kDa, 9.851 |
| Gene length, protein length | 579 bp, 193 aa |
| Immediate neighbours | fruA, ykoA |
| Sequences | Protein DNA Advanced_DNA |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
protein secretion, membrane proteins
This gene is a member of the following regulons
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)
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- 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
- Sigma factor:
- Regulation:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Jan Maarten van Dijl, Groningen, Netherlands
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)
