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
AMP25368.1X-Pro dipeptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (374 aa)    
Predicted Functional Partners:
efp
Elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
  
 
 0.854
atpE
ATP F0F1 synthase subunit C; 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.
  
  
 0.851
fbiA
2-phospho-L-lactate transferase; Catalyzes the transfer of the phosphoenolpyruvate moiety from enoylpyruvoyl-2-diphospho-5'-guanosine (EPPG) to 7,8-didemethyl-8- hydroxy-5-deazariboflavin (FO) with the formation of dehydro coenzyme F420-0 and GMP.
  
  
 0.828
AMP25367.1
Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.810
nusB
Antitermination protein NusB; Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
     
 0.809
AMP25371.1
Antitermination protein NusB; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.806
aroQ
3-dehydroquinate dehydratase; Catalyzes a trans-dehydration via an enolate intermediate. Belongs to the type-II 3-dehydroquinase family.
 
 
  0.776
fbiB
F420-0--gamma-glutamyl ligase; Bifunctional enzyme that catalyzes the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L- lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2- dependent reduction of dehydro-F420-0 to form F420-0. In the N-terminal section; belongs to the CofE family.
  
  
 0.770
fbiC
FO synthase; 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase; catalyzes radical-mediated transfer of hydroxybenzyl group from 4-hydroxyphenylpyruvate (HPP) to 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione to form 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO); functions in F420 biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.759
rplC
50S ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family.
      
 0.757
Your Current Organism:
Mycobacterium simiae
NCBI taxonomy Id: 1784
Other names: ATCC 25275, CCUG 29114, CCUG 42427, CIP 104531, DSM 44165, JCM 12377, M. simiae, Mycobacterium habana
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