Pfam: Trigger_C

Protein families database of alignments and HMMs

  Trigger_C  

Accession number: PF05698
Bacterial trigger factor protein (TF) C-terminus
In the E. coli cytosol, a fraction of the newly synthesised proteins requires the activity of molecular chaperones for folding to the native state. The major chaperones implicated in this folding process are the ribosome-associated Trigger Factor (TF), and the DnaK and GroEL chaperones with their respective co-chaperones. Trigger Factor is an ATP-independent chaperone and displays chaperone and peptidyl-prolyl-cis-trans-isomerase (PPIase) activities in vitro. It is composed of at least three domains, an N-terminal domain which mediates association with the large ribosomal subunit, a central substrate binding and PPIase domain with homology to FKBP proteins, and a C-terminal domain of unknown function. The positioning of TF at the peptide exit channel, together with its ability to interact with nascent chains as short as 57 residues renders TF a prime candidate for being the first chaperone that binds to the nascent polypeptide chains [1]. This family represents the C-terminal region of the protein.

INTERPRO description (entry IPR008880)
In the Escherichia coli cytosol, a fraction of the newly synthesised proteins requires the activity of molecular chaperones for folding to the native state. The major chaperones implicated in this folding process are the ribosome-associated Trigger Factor (TF), and the DnaK and GroEL chaperones with their respective co-chaperones. Trigger Factor is an ATP-independent chaperone and displays chaperone and peptidyl-prolyl-cis-trans-isomerase (PPIase) activities in vitro. It is composed of at least three domains, an N-terminal domain which mediates association with the large ribosomal subunit, a central substrate binding and PPIase domain with homology to FKBP proteins, and a C-terminal domain of unknown function. The positioning of TF at the peptide exit channel, together with its ability to interact with nascent chains as short as 57 residues renders TF a prime candidate for being the first chaperone that binds to the nascent polypeptide chains MEDLINE:22493129. These sequences contain the C-terminal domain.
QuickGO
PROCESS :protein transport (GO:0015031)

Alignment Domain organisation
Seed (56)  Full (122)

Format

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Seed (56)  Full (122)

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Species DistributionPhylogenetic tree
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Seed (56)  Full (122)

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Database References
PDB 1hxv (fa;) [CATH-PDBSUM|SCOP-UK|SCOP-USA|MSD]
SYSTERSTrigger_C
PANDITTrigger_C

Literature References
1.
Trigger Factor and DnaK possess overlapping substrate pools and binding specificities.
Deuerling E, Patzelt H, Vorderwulbecke S, Rauch T, Kramer G, Schaffitzel E, Mogk A, Schulze-Specking A, Langen H, Bukau B;
Mol Microbiol 2003;47:1317-1328.
Pfam specific information
Author of entryMoxon SJ
Type definitionFamily
Alignment method of seedClustalw
Source of seed membersPfam-B_8447 (release 8.0)
Average Length172.8
Average %id23
Average Coverage39.44%

HMMER build information
 Pfam_ls  [Download HMM]Pfam_fs  [Download HMM]
Gathering cutoff 25.0 25.0; 25.0 25.0
Trusted cutoff58.7 58.7; 43.2 29.7
Noise cutoff21.8 21.8; 22.8 22.8
Build method of HMMhmmbuild -F HMM_ls SEED
hmmcalibrate --seed 0 HMM_ls
hmmbuild -f -F HMM_fs SEED
hmmcalibrate --seed 0 HMM_fs

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