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bacbr-tycc

Bacillus brevis; Brevibacillus parabrevis, Tyrocidine synthetase III ATP-dependent asparagine adenylase, Asparagine activase, Thioesterase domain

Comment

Other strains: Bacillus brevis\; Brevibacillus parabrevis

Relationship

Family : Thioesterase

Block : X

Position in NCBI Life Tree : Bacillus brevis

Molecular evidence

No mutation

No structure

No kinetic

No disease

No substrate

No inhibitor

Database

Sequence

Peptide

RNVFCFTPIG AQSVYYQKLA AEIQGVSLYS FDFIQDDNRM EQYIAAITAI DPSGPYTLMG YSSGGNLAFE VAKELEERGY GVTDIILFDS YWKDKAIERT VAETENDIAQ LFAEIGENTE MFNMTQEDFQ LYAANEFVKQ SFVRKTVSYV MFHNNLVNTG MTTAAIHLIQ SELEADEEAP VAAKWNESAW ANATQRLLTY SGHGIHSRML AGDYASQNAS ILQNILQELF ILK

References

Title : Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases - Weber_2000_Structure_8_407
Author(s) : Weber T , Baumgartner R , Renner C , Marahiel MA , Holak TA
Ref : Structure , 8 :407 , 2000
Abstract : Weber_2000_Structure_8_407
ESTHER : Weber_2000_Structure_8_407
PubMedSearch : Weber_2000_Structure_8_407
PubMedID: 10801488
Gene_locus related to this paper: bacbr-tycc

Title : The tyrocidine biosynthesis operon of Bacillus brevis: complete nucleotide sequence and biochemical characterization of functional internal adenylation domains - Mootz_1997_J.Bacteriol_179_6843
Author(s) : Mootz HD , Marahiel MA
Ref : Journal of Bacteriology , 179 :6843 , 1997
Abstract : Mootz_1997_J.Bacteriol_179_6843
ESTHER : Mootz_1997_J.Bacteriol_179_6843
PubMedSearch : Mootz_1997_J.Bacteriol_179_6843
PubMedID: 9352938
Gene_locus related to this paper: bacbr-tycc , bacbr-TYCF