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
yetAPutative enzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (857 aa)    
Predicted Functional Partners:
yesY
Rhamnogalacturonan acetylesterase; May play a role in the degradation of rhamnogalacturonan derived from plant cell walls. Probably has broad substrate specificity and may degrade several types of acetylated substrates. Belongs to the 'GDSL' lipolytic enzyme family.
 
 
 0.939
cdoA
Cysteine dioxygenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
      
 0.920
rhgX
Rhamnogalacturonan exolyase YesX; Pectinolytic enzyme that degrades type I rhamnogalacturonan from plant cell walls and releases disaccharide products. Degrades rhamnogalacturonan, polygalacturonic acid and pectic acid. Has very low activity on pectin ; Belongs to the polysaccharide lyase 11 family.
 
    0.894
rhgT
Rhamnogalacturonan acetylesterase; May play a role in the degradation of type I rhamnogalacturonan derived from plant cell walls. This enzyme has a broad substrate specificity, and shows strong preference for glucose pentaacetate, beta-naphthylacetate, and p-nitrophenyl acetate (pNPA). Also active toward acetylated xylan.
 
 
 0.875
lplA
Lipoprotein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type lp: lipoprotein.
 
    0.866
rhgW
Rhamnogalacturonan endolyase; Pectinolytic enzyme that degrades type I rhamnogalacturonan from plant cell walls and releases oligosaccharide products. Degrades rhamnogalacturonan, polygalacturonic acid, pectic acid and pectin ; Belongs to the polysaccharide lyase 11 family.
 
    0.855
yxiM
Putative esterase (lipoprotein); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the 'GDSL' lipolytic enzyme family.
 
 
 
 0.843
pelC
Secreted pectate lyase; Catalyzes the depolymerization of both polygalacturonate and pectins of methyl esterification degree from 22 to 89%, with an endo mode of action. In contrast to the majority of pectate lyases, displays high activity on highly methylated pectins. Is also able to cleave trigalacturonate to galacturonic acid and unsaturated digalacturonate. Belongs to the polysaccharide lyase 3 family.
 
 
 0.801
rhgH
Rhamnogalacturonan hydrolase; Catalyzes the hydrolysis of unsaturated rhamnogalacturonan disaccharide to yield unsaturated D-galacturonic acid and L-rhamnose. It cannot act on unsaturated glucuronyl hydrolase (UGL) substrates containing unsaturated D-glucuronic acid at the non-reducing terminus, although the active pockets of YesR and UGL are very similar. Belongs to the glycosyl hydrolase 105 family.
 
  
 0.759
rhgZ
Beta-galacturonidase; May play a role in the degradation of rhamnogalacturonan derived from plant cell walls; Belongs to the glycosyl hydrolase 42 family.
 
    0.748
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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