Difference between revisions of "SecA"
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* '''Cofactor(s):''' magnesium | * '''Cofactor(s):''' magnesium | ||
− | * '''Effectors of protein activity:''' anionic phospholipids, preprotein, SecY | + | * '''Effectors of protein activity:''' anionic phospholipids, preprotein, SecY, signal peptides (even when added in trans) |
* '''Interactions:''' [[SecA]]-[[Ffh]], [[CsaA]]-[[SecA]], [[SecA]]-[[SecY]], [[SecA]]-[[SecA]] | * '''Interactions:''' [[SecA]]-[[Ffh]], [[CsaA]]-[[SecA]], [[SecA]]-[[SecY]], [[SecA]]-[[SecA]] |
Revision as of 10:16, 14 December 2009
- 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 |
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
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Contents
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)
- 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