STRINGSTRING
recA recA dinB dinB lexA lexA tagC tagC
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:
recAMultifunctional SOS repair factor; Multifunctional protein involved in homologous recombination, DNA repair and competence. Can catalyze the hydrolysis of (d)ATP in the presence of single-stranded DNA; prefers dATP at least in vitro, catalyzes the dATP-dependent uptake of single- stranded DNA by duplex DNA, and the dATP-dependent hybridization of homologous single-stranded DNAs (strand exchange). RecA-ATP cannot catalyze homologous DNA strand exchange; SsbA and DprA activate strand exchange by RecA-ATP. It interacts with LexA causing its activation and leading to its autocatalytic clea [...] (348 aa)
dinBNuclease inhibitor; Evidence 2b: Function of strongly homologous gene; regulator. (172 aa)
lexATranscriptional repressor of the SOS regulon; Represses dinA, dinB, dinC, recA genes and itself by binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'; some genes have a tandem consensus sequence and their binding is cooperative. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair; autocleavage is maximal at pH 11 in the absence of RecA and ssDNA. (205 aa)
tagCPutative polyglycerol phosphate assembly and export protein (teichoic acid biosynthesis); Unknown. Might be involved in poly(glycerol phosphate) teichoic acid biosynthesis. (442 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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