STRINGSTRING
cotB cotB hag hag fliD fliD yfiN yfiN amyE amyE cotH cotH cotG cotG
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:
cotBSpore coat protein (outer); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type s: structure. (380 aa)
hagFlagellin protein; Flagellin is the subunit which polymerizes to form the filaments of bacterial flagella. Assembly into flagella requires FliW. Acts as a homeostatic autoinhibitory regulator to control its own cytoplasmic levels. Partner switching by flagellin between FliW and CsrA provides a flagellar assembly checkpoint to tightly control the timing of flagellin synthesis. Flagellin binds to assembly factor FliW, freeing translation regulator CsrA to repress translation of the flagellin mRNA. When the flagellar hook is assembled flagellin is secreted, depleting intracellular flagell [...] (304 aa)
fliDFlagellar hook-associated capping protein 2 (HAP2); Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end (By similarity); Belongs to the FliD family. (498 aa)
yfiNPutative ABC transporter (permease); Required for resistance to linearmycins, a family of antibiotic-specialized metabolites produced by some streptomycetes. Part of the ABC transporter complex LnrLMN that probably facilitates linearmycin removal from the membrane. Responsible for the translocation of the substrate across the membrane. Also mediates KinC-dependent biofilm morphology ; Belongs to the ABC-2 integral membrane protein family. (385 aa)
amyEAlpha-amylase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glycosyl hydrolase 13 family. (659 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)
cotGSpore morphogenetic protein; May be a morphogenetic protein that is required for the incorporation of protein CotB into the spore coat. (195 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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