CsaA

• Description: molecular chaperone involved in protein secretion
  
  

Gene name	csaA
Synonyms
Essential	no
Product	molecular chaperone
Function	protein secretion
Gene expression levels in SubtiExpress: csaA
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
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, membrane proteins

The gene

Basic information

• Locus tag: BSU19040

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:

• Expression browser: csaA PubMed

• 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)