Difference between revisions of "SecA"

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(References)
(Extended information on the protein)
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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
SecA context.gif
This image was kindly provided by SubtiList



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

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