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
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[Homology]
Score
Aaci_1992MiaB-like tRNA modifying enzyme; KEGG: sat:SYN_00797 tRNA 2-methylthioadenosine synthase -like protein; TIGRFAM: MiaB-like tRNA modifying enzyme; RNA modification enzyme, MiaB family; PFAM: Protein of unknown function UPF0004; Radical SAM domain protein; SMART: Elongator protein 3/MiaB/NifB. (471 aa)    
Predicted Functional Partners:
prmA
Ribosomal protein L11 methyltransferase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family.
  
  
 0.914
Aaci_1993
Protein of unknown function DUF558; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
  
  
 0.877
deoC
Deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5- phosphate; Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.
  
    0.800
dnaJ
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...]
  
 
 0.751
Aaci_1322
Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
  
  
 0.629
Aaci_1999
Oxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family.
 
  
 0.627
Aaci_2676
ATPase-like, ParA/MinD; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family.
  
   
 0.598
rlmN
Radical SAM enzyme, Cfr family; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family.
 
  
 0.549
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
     
 0.516
lepA
GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner.
  
    0.482
Your Current Organism:
Alicyclobacillus acidocaldarius DSM 446
NCBI taxonomy Id: 521098
Other names: A. acidocaldarius subsp. acidocaldarius DSM 446, Alicyclobacillus acidocaldarius subsp. acidocaldarius ATCC 27009, Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446, Alicyclobacillus acidocaldarius subsp. acidocaldarius IFO 15652, Alicyclobacillus acidocaldarius subsp. acidocaldarius JCM 5260, Alicyclobacillus acidocaldarius subsp. acidocaldarius NBRC 15652, Alicyclobacillus acidocaldarius subsp. acidocaldarius NCIB 11725, Alicyclobacillus acidocaldarius subsp. acidocaldarius str. DSM 446, Alicyclobacillus acidocaldarius subsp. acidocaldarius strain DSM 446
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