STRINGSTRING
Aaci_0778 Aaci_0778 Aaci_0779 Aaci_0779 lepA lepA prfC prfC rnhB rnhB atpE atpE Aaci_0781 Aaci_0781 Aaci_1649 Aaci_1649 Aaci_1426 Aaci_1426 secF secF Aaci_0777 Aaci_0777
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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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Aaci_0778TIGRFAM: signal peptidase I; PFAM: Peptidase S24, S26A and S26B, conserved region; KEGG: pfs:PFLU1059 signal peptidase I; Belongs to the peptidase S26 family. (191 aa)    
Predicted Functional Partners:
Aaci_0779
PFAM: aldo/keto reductase; KEGG: bxe:Bxe_B0844 putative aldo/keto reductase.
  
  
 0.740
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.
 
 
 0.726
prfC
Peptide chain release factor 3; Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. PrfC subfamily.
  
  
 0.681
rnhB
Ribonuclease H; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
  
  
 0.616
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.
    
 0.609
Aaci_0781
PFAM: peptidase M14 carboxypeptidase A; SMART: peptidase M14 carboxypeptidase A; KEGG: aeh:Mlg_1727 peptidase M14, carboxypeptidase A.
     
 0.600
Aaci_1649
PFAM: ATP dependent DNA ligase; KEGG: bch:Bcen2424_6876 ATP dependent DNA ligase.
    
 0.573
Aaci_1426
KEGG: acp:A2cp1_1249 membrane-associated zinc metalloprotease; TIGRFAM: membrane-associated zinc metalloprotease; PFAM: peptidase M50; SMART: PDZ/DHR/GLGF domain protein.
 
  
 0.567
secF
Protein-export membrane protein SecF; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
  
  
 0.565
Aaci_0777
Hypothetical protein.
       0.499
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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