Difference between revisions of "SecA"
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 10:09, 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
Dorothy M Kim, Haiyan Zheng, Yuanpeng J Huang, Gaetano T Montelione, John F Hunt
ATPase active-site electrostatic interactions control the global conformation of the 100 kDa SecA translocase.
J Am Chem Soc: 2013, 135(8);2999-3010
[PubMed:23167435]
[WorldCat.org]
[DOI]
(I p)
Hiroshi Kakeshita, Yasushi Kageyama, Katsutoshi Ara, Katsuya Ozaki, Kouji Nakamura
Enhanced extracellular production of heterologous proteins in Bacillus subtilis by deleting the C-terminal region of the SecA secretory machinery.
Mol Biotechnol: 2010, 46(3);250-7
[PubMed:20574771]
[WorldCat.org]
[DOI]
(I p)
Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983]
[WorldCat.org]
[DOI]
(I p)
Jan D H Jongbloed, Haike Antelmann, Michael Hecker, Reindert Nijland, Sierd Bron, Ulla Airaksinen, Frens Pries, Wim J Quax, Jan Maarten van Dijl, Peter G Braun
Selective contribution of the twin-arginine translocation pathway to protein secretion in Bacillus subtilis.
J Biol Chem: 2002, 277(46);44068-78
[PubMed:12218047]
[WorldCat.org]
[DOI]
(P p)
M Herbort, M Klein, E H Manting, A J Driessen, R Freudl
Temporal expression of the Bacillus subtilis secA gene, encoding a central component of the preprotein translocase.
J Bacteriol: 1999, 181(2);493-500
[PubMed:9882663]
[WorldCat.org]
[DOI]
(P p)
K Bunai, K Yamada, K Hayashi, K Nakamura, K Yamane
Enhancing effect of Bacillus subtilis Ffh, a homologue of the SRP54 subunit of the mammalian signal recognition particle, on the binding of SecA to precursors of secretory proteins in vitro.
J Biochem: 1999, 125(1);151-9
[PubMed:9880811]
[WorldCat.org]
[DOI]
(P p)
-1-
-2-