CsaA

• Description: molecular chaperone involved in protein secretion
  
  

Gene name	csaA
Synonyms
Essential	no
Product	molecular chaperone
Function	protein secretion
Interactions involving this protein in SubtInteract: CsaA
Metabolic function and regulation of this protein in SubtiPathways: Protein secretion
MW, pI	11 kDa, 8.691
Gene length, protein length	330 bp, 110 aa
Immediate neighbours	bsrF, yobQ
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

protein secretion, membrane proteins

The gene

Basic information

• Locus tag: BSU19040

Expression

Phenotypes of a mutant

From unsuccessful trials to knock out the gene it was concluded that csaA apparently is essential. However, in a conditional mutant (Pspac-csaA), depletion of the gene product is not lethal. But secretion of some proteins including SdpC was reported to be affected unter such conditions.PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Secretion associated chaperone. Assumed functional analogue of E. coli SecB

• Protein family: FIG1 subfamily (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains: CsaA contains a tRNA binding domain.

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • CsaA-SdpC PubMed
  • CsaA-SecA PubMed
  • CsaA-CsaA

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

Database entries

• Structure: 2NZO

• UniProt: P37584

• KEGG entry: [2]

• E.C. number:

Additional information

The functional entity of CsaA is the homodimer.

Expression and regulation

• Operon:

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant: Pspac-csaA PubMed

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Yuliya A Shapova, Mark Paetzel
Crystallographic analysis of Bacillus subtilis CsaA.
Acta Crystallogr D Biol Crystallogr: 2007, 63(Pt 4);478-85
[PubMed:17372352] [WorldCat.org] [DOI] (P p)

Dirk Linde, Rudolf Volkmer-Engert, Sandra Schreiber, Jörg P Müller
Interaction of the Bacillus subtilis chaperone CsaA with the secretory protein YvaY.
FEMS Microbiol Lett: 2003, 226(1);93-100
[PubMed:13129613] [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)

Jörg P Müller, Sierd Bron, Gerard Venema, Jan Maarten van Dijl
Chaperone-like activities of the CsaA protein of Bacillus subtilis.
Microbiology (Reading): 2000, 146 ( Pt 1);77-88
[PubMed:10658654] [WorldCat.org] [DOI] (P p)