Difference between revisions of "SecA"

From SubtiWiki
Jump to: navigation, search
(Extended information on the protein)
(Basic information/ Evolution)
Line 54: Line 54:
 
=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
* '''Catalyzed reaction/ biological activity:'''  
+
* '''Catalyzed reaction/ biological activity:''' ATP -> ADP + Pi + preprotein translocation
  
* '''Protein family:''' secA family (according to Swiss-Prot)
+
* '''Protein family:''' SecA family (according to Swiss-Prot)
  
* '''Paralogous protein(s):'''
+
* '''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 ===
 
=== Extended information on the protein ===

Revision as of 11:42, 2 June 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
SecA context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Coordinates:

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
  • Localization: cell membrane (according to Swiss-Prot)

Database entries

  • Structure: 1TF5 (open structure), 2IBM
  • 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

  1. Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
  2. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed