SecA

• Description: preprotein translocase subunit (ATPase), required for membrane targeting of DivIVA
  
  

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: SecA
MW, pI	95 kDa, 5.34
Gene length, protein length	2523 bp, 841 aa
Immediate neighbours	prfB, yvyD
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

protein secretion, essential genes, membrane proteins

The gene

Basic information

• Locus tag: BSU35300

Phenotypes of a mutant

essential PubMed

Database entries

• BsubCyc: BSU35300

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • ATP -> ADP + Pi + preprotein translocation
  • required for membrane targeting of DivIVA PubMed

• 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:

• Cofactors: Mg

• Effectors of protein activity: anionic phospholipids, preprotein, SecY, signal peptides (even when added in trans) PubMed

• Interactions:
  • (SecY-SecE-SecG)2-SecA2 PubMed
  • SecA-Ffh PubMed
  • CsaA-SecA PubMed
  • DivIVA-SecA PubMed

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

Database entries

• BsubCyc: BSU35300

• 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

• Operon: secA-prfB PubMed

• Expression browser: secA PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:
  • subject to Clp-dependent proteolysis upon glucose starvation PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 945 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 2829 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 411 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 395 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 564 PubMed

Biological materials

• Mutant: Pspac-secA PubMed

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody: