Difference between revisions of "SecA"
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=== Database entries === | === Database entries === | ||
− | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1TF5 1TF5] (open structure), [http://www.rcsb.org/pdb/explore.do?structureId=2IBM 2IBM] | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1TF5 1TF5] (open structure), [http://www.rcsb.org/pdb/explore.do?structureId=2IBM 2IBM], [http://www.rcsb.org/pdb/explore/explore.do?pdbId=3DL8 3DL8] () structure of the ([[SecY]]-[[SecE]]-[[SecG]])-[[SecA]] complex {{PubMed|18923516}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P28366 P28366] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P28366 P28366] |
Revision as of 10:39, 4 June 2010
- 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
|
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) PubMed
- Localization: cell membrane (according to Swiss-Prot)
Database entries
- Structure: 1TF5 (open structure), 2IBM, 3DL8 () structure of the (SecY-SecE-SecG)-SecA complex PubMed
- 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