close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING newly available directed regulatory networks a new typed view showing functional, physical, and regulatory edges in one network new clustering options and cluster-based layouts … and much more!
Explore STRING v12.5 →
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
AEB83306.1PFAM: Lytic transglycosylase-like, catalytic; KEGG: ajs:Ajs_0847 lytic transglycosylase, catalytic. (214 aa)    
Predicted Functional Partners:
proS
Prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves dea [...]
       0.837
rppH
NUDIX hydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily.
   
   0.695
AEB86911.1
KEGG: ajs:Ajs_4050 peptidoglycan-binding LysM; PFAM: Peptidoglycan-binding lysin domain; SMART: Peptidoglycan-binding Lysin subgroup.
 
   
 0.680
AEB83214.1
KEGG: ajs:Ajs_0732 pilus assembly protein, PilO.
  
     0.670
AEB85535.1
PFAM: Type IV pilus assembly PilZ; KEGG: dia:Dtpsy_1985 type IV pilus assembly PilZ.
  
     0.644
AEB83212.1
TIGRFAM: Type IV pilus assembly protein PilM; KEGG: ajs:Ajs_0730 type IV pilus assembly protein PilM.
  
     0.617
AEB83677.1
KEGG: dia:Dtpsy_2621 putative transmembrane protein.
  
     0.611
AEB83213.1
PFAM: Fimbrial assembly; KEGG: ajs:Ajs_0731 fimbrial assembly family protein.
  
     0.608
AEB83707.1
TIGRFAM: Motility protein FimV, N-terminal; Motility protein FimV, C-terminal; KEGG: ajs:Ajs_3236 putative transmembrane protein.
  
     0.598
AEB83215.1
PFAM: Pilus assembly protein PilP; KEGG: dia:Dtpsy_0702 pilus assembly protein PilP.
  
     0.593
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
Server load: low (32%) [HD]