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tcpJ

Gene
tcpJ
Protein
Dipeptidase tcpJ
Organism
Claviceps purpurea (strain 20.1)
Length
425 amino acids
Function
Dipeptidase; part of the gene cluster that mediates the biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) lacking the reactive thiol group important for toxicity (PubMed:27390873). Firstly, L-tyrosine is prenylated by tcpD, before undergoing condensation with L-glycine in a reaction catalyzed by the NRPS tcpP leading to the diketopiperazine (DKP) backbone (PubMed:27390873). Afterwards the alpha-carbon of tyrosine is oxidized by the cytochrome P450 tcpC to form a hydroxyl group (PubMed:27390873). However, in contrast other ETP biosynthesis pathways studied so far, tcpC is not able to bishydroxylate the DKP at both alpha-carbon positions, but hydroxylates the alpha-carbon of the tyrosine part and the nitrogen of the glycine part (PubMed:27390873). The next steps involve an alpha,beta-elimination reaction catalyzed by tcpI, a methylation by the methyltransferase tcpN the action of the four enzyme cascade tcpG/K/J/I (PubMed:27390873). Due to a dysfunctional cytochrome P450 monooxygenase tcpC, the pathway leads to the biosynthesis of probable non-toxic metabolites lacking the reactive thiol group (PubMed:27390873).
Similarity
Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family.
Mass
47.461 kDa
Sequence
MATAAQPSLELALELMSKVPLIGNISQSTHKIPIQCTGLTREQDGHNDWMHMIRAYYDFQVDDRFQPTKDLAGHVDLKRLVQGRAGAVFWSVYVECPKGENDFSDAVHHASMRDTFQQIDLLQRIMELYSDRMEMAHKADDVMRIFRSGKCASLMGAEGLHQLGNSSSVLRIFHRLGVRYVTLAHAKNNLYVDSATSEAPIHHGLSPQGRDMVREMNRIGMIVDLSHVSEKAMVDALDVSLAPVIFSHSSAYALVPHVRNVPDHVLDRLKQNRGIIMISFIPWLTNKDPEKATVENVVDHVLHVGNRIGFDHLGLGSDFDGMPSHVQGLEDVSKYPNVVAAMLQRGISTENVEKIMGMNVIRVLREVEDVAASQKGLLPVLEDAVPQLWDDGIRAYVKKLYPHAEHDRTGASETTTVDKAIEKDV

Gene
tcpJ
Protein
Type 4 prepilin-like proteins leader peptide-processing enzyme
Organism
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Length
253 amino acids
Function
Cleaves type-4 fimbrial leader sequence and methylates the N-terminal (generally Phe) residue. Processes the TcpA pilin precursor during membrane translocation.
Similarity
Belongs to the peptidase A24 family.
Mass
29.337 kDa
Sequence
MEYVYLILFSIVSLILGSFSNVVIYRLPRKILLKNHFFYDIDSNRSMCPKCGNKISWYDNVPLLSYLLLHGKCRHCDEKISLSYFIVELSFFIIAFPIYWLSTDWVDSFVLLGLYFILFNLFVIDFKSMLLPNLLTYPIFMLAFIYVQQNPALTVESSIIGGFAAFIISYVSNFIVRLFKRIDVMGGGDIKLYTAIGTLIGVEFVPYLFLLSSIIAFIHWFFARVSCRYCLYIPLGPSIIISFVIVFFSIRLM

Gene
tcpJ
Protein
Type 4 prepilin-like proteins leader peptide-processing enzyme
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Length
253 amino acids
Function
Cleaves type-4 fimbrial leader sequence and methylates the N-terminal (generally Phe) residue. Processes the TcpA pilin precursor during membrane translocation.
Similarity
Belongs to the peptidase A24 family.
Mass
29.337 kDa
Sequence
MEYVYLILFSIVSLILGSFSNVVIYRLPRKILLKNHFFYDIDSNRSMCPKCGNKISWYDNVPLLSYLLLHGKCRHCDEKISLSYFIVELSFFIIAFPIYWLSTDWVDSFVLLGLYFILFNLFVIDFKSMLLPNLLTYPIFMLAFIYVQQNPALTVESSIIGGFAAFIISYVSNFIVRLFKRIDVMGGGDIKLYTAIGTLIGVEFVPYLFLLSSIIAFIHWFFARVSCRYCLYIPLGPSIIISFVIVFFSIRLM