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
PC1_1135Peroxiredoxin; PFAM: alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen; Redoxin domain protein; KEGG: eca:ECA1260 thioredoxin-dependent thiol peroxidase. (155 aa)    
Predicted Functional Partners:
PC1_1136
PFAM: amino acid-binding ACT domain protein; KEGG: eca:ECA1261 glycine cleavage system transcriptional repressor.
  
    0.687
bepA
Peptidase M48 Ste24p; Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state.
  
    0.557
norV
Beta-lactamase domain protein; Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the NorW at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase; In the N-terminal section; belongs to the zinc metallo- hydrolase group 3 family.
  
  
 0.495
PC1_1288
Putative ATPase; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family.
  
  
 0.475
PC1_1717
TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: eca:ECA2649 thioredoxin reductase.
 
  
 0.470
PC1_1025
Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.
     
 0.468
PC1_1133
TIGRFAM: arsenate reductase; PFAM: arsenate reductase and related; KEGG: eca:ECA1258 putative arsenate reductase.
  
    0.467
msrA
Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
 
  
 0.463
bamC
NlpBDapX family lipoprotein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
 
    0.462
PC1_2597
TIGRFAM: flagellar basal-body rod protein FlgC; PFAM: flagellar basal body rod protein; protein of unknown function DUF1078 domain protein; KEGG: eca:ECA1703 flagellar basal body rod protein FlgC; Belongs to the flagella basal body rod proteins family.
    
   0.443
Your Current Organism:
Pectobacterium carotovorum
NCBI taxonomy Id: 561230
Other names: P. carotovorum subsp. carotovorum PC1, Pectobacterium carotovorum subsp. carotovorum PC1, Pectobacterium carotovorum subsp. carotovorum str. PC1, Pectobacterium carotovorum subsp. carotovorum strain PC1
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