SecY

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Gene name secY
Synonyms
Essential yes PubMed
Product preprotein translocase subunit
Function protein secretion
Gene expression levels in SubtiExpress: secY
Interactions involving this protein in SubtInteract: SecY
Metabolic function and regulation of this protein in SubtiPathways:
SecY
MW, pI 47 kDa, 10.209
Gene length, protein length 1293 bp, 431 aa
Immediate neighbours rplO, adk
Sequences Protein DNA DNA_with_flanks
Genetic context
SecY context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SecY expression.png















Categories containing this gene/protein

protein secretion, essential genes, membrane proteins, universally conserved proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU01360

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: secY/SEC61-alpha family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [2]
  • E.C. number:

Additional information

universally conserved protein

Expression and regulation

  • Operon: rplO-secY-adk-map
  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

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)

Juri Niño Bach, Marc Bramkamp
Flotillins functionally organize the bacterial membrane.
Mol Microbiol: 2013, 88(6);1205-17
[PubMed:23651456] [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)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I 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)

J W Suh, S A Boylan, S H Oh, C W Price
Genetic and transcriptional organization of the Bacillus subtilis spc-alpha region.
Gene: 1996, 169(1);17-23
[PubMed:8635744] [WorldCat.org] [DOI] (P p)

R Breitling, B Schlott, D Behnke
Modulation of the spc operon affects growth and protein secretion in Bacillus subtilis.
J Basic Microbiol: 1994, 34(3);145-55
[PubMed:8071801] [WorldCat.org] [DOI] (P p)

J W Suh, S A Boylan, S M Thomas, K M Dolan, D B Oliver, C W Price
Isolation of a secY homologue from Bacillus subtilis: evidence for a common protein export pathway in eubacteria.
Mol Microbiol: 1990, 4(2);305-14
[PubMed:2110998] [WorldCat.org] [DOI] (P p)