Difference between revisions of "SecA"
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− | + | '''Additional publications:''' {{PubMed|20574771}} | |
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 10:13, 23 November 2012
- Description: preprotein translocase subunit (ATPase)
Gene name | secA |
Synonyms | div, div-341, ts-341 |
Essential | yes PubMed |
Product | preprotein translocase subunit (ATPase) |
Function | protein secretion |
Gene expression levels in SubtiExpress: secA | |
Interactions involving this protein in SubtInteract: SecA | |
Metabolic function and regulation of this protein in SubtiPathways: Protein secretion | |
MW, pI | 95 kDa, 5.34 |
Gene length, protein length | 2523 bp, 841 aa |
Immediate neighbours | prfB, yvyD |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
protein secretion, essential genes, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU35300
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP -> ADP + Pi + preprotein translocation
- Protein family: SecA family (according to Swiss-Prot)
- Paralogous protein(s): none in Bacillus, some species have a paralogous secA gene named secA2 that has an altered substrate range
Extended information on the protein
- Kinetic information:
- Domains: nucleotide binding domain, preprotein binding domain, IRA2 domain, scaffold domain, wing domain, IRA1 domain, C-terminal domain
- Modification:
- Cofactor(s): magnesium
- Effectors of protein activity: anionic phospholipids, preprotein, SecY, signal peptides (even when added in trans) PubMed
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- UniProt: P28366
- KEGG entry: [3]
- E.C. number:
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Additional publications: PubMed