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:

References

Sven Halbedel, Maki Kawai, Reinhard Breitling, Leendert W Hamoen
SecA is required for membrane targeting of the cell division protein DivIVA in vivo.
Front Microbiol: 2014, 5;58
[PubMed:24592260] [WorldCat.org] [DOI] (P e)

Chun-Kai Yang, Chung-Dar Lu, Phang C Tai
Differential expression of secretion machinery during bacterial growth: SecY and SecF decrease while SecA increases during transition from exponential phase to stationary phase.
Curr Microbiol: 2013, 67(6);682-7
[PubMed:23852076] [WorldCat.org] [DOI] (I p)

Jianmei Cui, Jinshan Jin, Ying-Hsin Hsieh, Hsiuchin Yang, Bowen Ke, Krishna Damera, Phang C Tai, Binghe Wang
Design, synthesis and biological evaluation of rose bengal analogues as SecA inhibitors.
ChemMedChem: 2013, 8(8);1384-93
[PubMed:23794293] [WorldCat.org] [DOI] (I p)

Sarah M Auclair, Donald B Oliver, Ishita Mukerji
Defining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transfer.
Biochemistry: 2013, 52(14);2388-401
[PubMed:23484952] [WorldCat.org] [DOI] (I p)

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)

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)