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
Xcel_0342PFAM: methyltransferase small; Methyltransferase type 12; KEGG: sus:Acid_0228 methyltransferase small; Belongs to the methyltransferase superfamily. (572 aa)    
Predicted Functional Partners:
prfA
Peptide chain release factor 1; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
  
 
 0.921
Xcel_0341
KEGG: Hypothetical protein CBG15581.
       0.773
Xcel_1124
KEGG: ank:AnaeK_4439 hypothetical protein.
    
 0.672
Xcel_0340
KEGG: hypothetical protein.
       0.590
atpE
ATP synthase F0, C subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
  
   0.530
atpH
ATP synthase F1, delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family.
  
   0.521
Xcel_1723
PFAM: Fmu (Sun) domain protein; NusB/RsmB/TIM44; KEGG: gme:Gmet_0066 Fmu, rRNA SAM-dependent methyltransferase:Nop2p; Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.
 
 
 0.511
Xcel_1312
Hypothetical protein; KEGG: met:M446_5885 adenylate/guanylate cyclase.
 
     0.503
topA
DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...]
       0.487
atpG
ATP synthase F1, gamma subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
  
   0.487
Your Current Organism:
Xylanimonas cellulosilytica
NCBI taxonomy Id: 446471
Other names: X. cellulosilytica DSM 15894, Xylanimonas cellulosilytica DSM 15894, Xylanimonas cellulosilytica str. DSM 15894, Xylanimonas cellulosilytica strain DSM 15894
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.