UniProt functional annotation for Q9RT21

UniProt code: Q9RT21.

Organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
Taxonomy: Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae; Deinococcus.
 
Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity). Probably changes conformation upon binding to the ribosome (maybe in particular due to interaction with L24, PubMed:16271892), exposing a hydrophobic crevice that is probably important for its chaperone activity (PubMed:16091460 and PubMed:16271892). {ECO:0000250}.
 
Catalytic activity: Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit: Binds to the 50S ribosomal subunit via interactions with ribosomal protein L23. Also interacts with 23S rRNA and proteins L24 and L29 when complexed with the ribosome (PubMed:16091460 and PubMed:16271892). {ECO:0000269|PubMed:16091460, ECO:0000269|PubMed:16271892}.
Subcellular location: Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm. {ECO:0000250}.
Domain: Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own. {ECO:0000250}.
Similarity: Belongs to the FKBP-type PPIase family. Tig subfamily. {ECO:0000305}.
Similarity: Contains 1 PPIase FKBP-type domain. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.