Accession | TIGR02222 |
Name | chap_CsaA |
Function | export-related chaperone protein CsaA |
Gene Symbol | csaA |
Trusted Cutoff | 119.65 |
Domain Trusted Cutoff | 119.65 |
Noise Cutoff | 94.40 |
Domain Noise Cutoff | 94.40 |
Isology Type | subfamily |
HMM Length | 107 |
Mainrole Category | Protein fate |
Subrole Category | Protein folding and stabilization |
Gene Ontology Term | GO:0005515: protein binding molecular_function |
| GO:0009306: protein secretion biological_process |
| GO:0050821: protein stabilization biological_process |
Author | Haft DH |
Entry Date | Jun 11 2004 2:54PM |
Last Modified | Apr 26 2012 8:11AM |
Comment | This HMM describes Bacillus subtilis CsaA, an export-related chaperone that interacts with the Sec system, and related proteins from a number of other bacteria and archaea. The crystal structure is known for the homodimer from Thermus thermophilus. |
References | RN [1]
RM 11157762
RT The crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus.
RA Kawaguchi S, Muller J, Linde D, Kuramitsu S, Shibata T, Inoue Y, Vassylyev DG, Yokoyama S.
RL EMBO J. 2001 Feb 1;20(3):562-9.
RN [2]
RM 13129613
RT Interaction of the Bacillus subtilis chaperone CsaA with the secretory protein YvaY.
RA Linde D, Volkmer-Engert R, Schreiber S, Muller JP.
RL FEMS Microbiol Lett. 2003 Sep 12;226(1):93-100. |