STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
tycBNon-ribosomal peptide synthetase; Activates the second to fourth amino acids in tyrocidine (in tyrocidine A, Pro, Phe, and D-Phe) and epimerizes the last one. (3588 aa)    
Predicted Functional Partners:
lgrD
Non-ribosomal peptide synthetase; Activates the 13th to the 16th (Trp, D-Leu, Trp and Gly) amino acids in linear gramicidin and catalyzes the formation of the peptide bond between them. This enzyme is also responsible for the epimerization of the 14th (D-Leu) amino acid. It also catalyzes the NAD(P)H-dependent reduction of the C-terminal glycine residue of the N- formylated 16-mer peptide, that binds to the peptidyl carrier domain of the terminal module of this protein, to form a peptidyl-aldehyde intermediate that is released from the enzyme complex.
 
0.999
lgrA
Non-ribosomal peptide synthetase; Activates valine (or leucine, but much less frequently), and then glycine and catalyzes the formation of the peptide bond in the first step of peptide synthesis. This enzyme may also play a role in N- formylation of the first amino acid residue in the synthesized dipeptide; Belongs to the ATP-dependent AMP-binding enzyme family.
 
 
0.999
KZE52227.1
AMP-dependent synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
0.999
KZE52230.1
Non-ribosomal peptide synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
0.999
KZE51914.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
 
0.999
tycA
Non-ribosomal peptide synthetase; In the first step of peptide synthesis this enzyme activates phenylalanine and racemizes it to the D-isomer.
 
 
0.999
tycC
Non-ribosomal peptide synthetase; Incorporates six amino acids (for tyrocidine A, Asn, Gln, Tyr, Val, Orn, and Leu) in their L-configuration into the peptide product; Belongs to the ATP-dependent AMP-binding enzyme family.
 
 
0.999
KZE43678.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
 
0.999
KZE43679.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
 0.999
KZE43681.1
Beta-ketoacyl synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
0.999
Your Current Organism:
Brevibacillus parabrevis
NCBI taxonomy Id: 54914
Other names: ATCC 10027, B. parabrevis, Bacillus parabrevis, CIP 103840, DSM 8376, IFO 12334, JCM 8506, LMG 15971, LMG:15971, NBRC 12334, NCIMB 13346, NRRL NRS-605, NRRL NRS-815
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