STRINGSTRING
yplQ yplQ cotX cotX cotB cotB cotJA cotJA cotJB cotJB cotJC cotJC cotZ cotZ cotG cotG cotY cotY cotD cotD cotE cotE recA recA cotH cotH cotW cotW
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.
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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:
yplQPutative membrane hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (213 aa)
cotXSpore coat protein (insoluble fraction); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process. (172 aa)
cotBSpore coat protein (outer); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type s: structure. (380 aa)
cotJAComponent of the inner spore coat; The cotJ operon proteins affect spore coat composition. They are either required for the normal formation of the inner layers of the coat or are themselves structural components of the coat. (82 aa)
cotJBComponent of the inner spore coat; The cotJ operon proteins affect spore coat composition. They are either required for the normal formation of the inner layers of the coat or are themselves structural components of the coat. (87 aa)
cotJCComponent of the inner spore coat; The cotJ operon proteins affect spore coat composition. They are either required for the normal formation of the inner layers of the coat or are themselves structural components of the coat. (189 aa)
cotZSpore coat protein (insoluble fraction, outermost layer); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type s: structure. (148 aa)
cotGSpore morphogenetic protein; May be a morphogenetic protein that is required for the incorporation of protein CotB into the spore coat. (195 aa)
cotYOuter spore coat protein (insoluble fraction); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process. (162 aa)
cotDSpore coat protein (inner); Evidence 1a: Function experimentally demonstrated in the studied strain; cell process. (75 aa)
cotEMorphogenic spore protein; Morphogenic protein required for the assembly of the outer coat of the endospore. Is also a regulatory protein for the expression of cotA, cotB, cotC, cotH and other genes encoding spore outer coat proteins. (181 aa)
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)
cotHSpore coat protein (inner); Involved in the assembly of several proteins in the inner and outer layer of the spore coat. Stabilizes CotC and CotU in the mother cell compartment of sporulating cells and promotes the assembly of both early and late forms of CotC-related polypeptides on the spore surface. Belongs to the CotH family. (362 aa)
cotWSpore coat protein (insoluble fraction); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type cp: cell process. (105 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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