SecA

• 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

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

• DBTBS entry: [1]

• SubtiList entry: [2]

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

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

• 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

Biological materials

• Mutant: Pspac-secA PubMed

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

Benedikt W Bauer, Tom A Rapoport
Mapping polypeptide interactions of the SecA ATPase during translocation.
Proc Natl Acad Sci U S A: 2009, 106(49);20800-5
[PubMed:19933328] [WorldCat.org] [DOI] (I p)

Giorgos Gouridis, Spyridoula Karamanou, Ioannis Gelis, Charalampos G Kalodimos, Anastassios Economou
Signal peptides are allosteric activators of the protein translocase.
Nature: 2009, 462(7271);363-7
[PubMed:19924216] [WorldCat.org] [DOI] (I p)

Jochen Zimmer, Tom A Rapoport
Conformational flexibility and peptide interaction of the translocation ATPase SecA.
J Mol Biol: 2009, 394(4);606-12
[PubMed:19850053] [WorldCat.org] [DOI] (I p)

Jochen Zimmer, Yunsun Nam, Tom A Rapoport
Structure of a complex of the ATPase SecA and the protein-translocation channel.
Nature: 2008, 455(7215);936-43
[PubMed:18923516] [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)

Haiyuan Ding, John F Hunt, Ishita Mukerji, Donald Oliver
Bacillus subtilis SecA ATPase exists as an antiparallel dimer in solution.
Biochemistry: 2003, 42(29);8729-38
[PubMed:12873133] [WorldCat.org] [DOI] (P p)

John F Hunt, Sevil Weinkauf, Lisa Henry, John J Fak, Paul McNicholas, Donald B Oliver, Johann Deisenhofer
Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA.
Science: 2002, 297(5589);2018-26
[PubMed:12242434] [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)

J P Müller, J Ozegowski, S Vettermann, J Swaving, K H Van Wely, A J Driessen
Interaction of Bacillus subtilis CsaA with SecA and precursor proteins.
Biochem J: 2000, 348 Pt 2(Pt 2);367-73
[PubMed:10816431] [WorldCat.org] (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)

H Takamatsu, S Fuma, K Nakamura, Y Sadaie, A Shinkai, S Matsuyama, S Mizushima, K Yamane
In vivo and in vitro characterization of the secA gene product of Bacillus subtilis.
J Bacteriol: 1992, 174(13);4308-16
[PubMed:1385592] [WorldCat.org] [DOI] (P p)