HMM Summary Page: TIGR02222

AccessionTIGR02222
Namechap_CsaA
Functionexport-related chaperone protein CsaA
Gene SymbolcsaA
Trusted Cutoff119.65
Domain Trusted Cutoff119.65
Noise Cutoff94.40
Domain Noise Cutoff94.40
Isology Typesubfamily
HMM Length107
Mainrole CategoryProtein fate
Subrole CategoryProtein folding and stabilization
Gene Ontology TermGO:0005515: protein binding molecular_function
GO:0009306: protein secretion biological_process
GO:0050821: protein stabilization biological_process
AuthorHaft DH
Entry DateJun 11 2004 2:54PM
Last ModifiedApr 26 2012 8:11AM
CommentThis 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.
ReferencesRN [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.