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
clpB2Putative ATP-dependent Clp protease, ATP-binding subunit ClpB. Homology to clpB of E. coli of 38% (sprot|CLPB_ECOLI). The protein is thought to be subunits of ATP-dependent proteases which act as chaperones to target the proteases to substrates. Pfam: ATPsae family associated with various cellular activites no signal peptide no TMHs; High confidence in function and specificity; Belongs to the ClpA/ClpB family. (906 aa)    
Predicted Functional Partners:
sciI
Putative cytoplasmic protein, sciI, 68% identity(80% similarity) to TrEMBL;Q93IS7. Has PF05943,Protein of unknown function (DUF877);IPR010269;This family consists of a number of uncharacterised bacterial proteins. The function of this family is unknown; High confidence in function and specificity.
 
 0.961
sciB
Putative cytoplasmic protein, sciB. TrEMBl;Q93IT4(36% identity) Has PF06996;Protein of unknown function (DUF1305);IPR010732; This family consists of several hypothetical bacterial proteins of around 300 residues in length. The function of this family is unknown although one member (Q93IT4) from Salmonella enterica is thought to be involved in virulence; Conserved hypothetical protein.
 
 
 0.947
azo1304
Hypothetical protein,63% identity (81% similarity) to TrEMBL;Q8XRT7. TrEMBL;Q7NR07(73% identity,86% similarity). Has (IPR010269)PF05943:Protein of unknown function (DUF877);This family consists of a number of uncharacterised bacterial proteins. The function of this family is unknown. No Signal peptide or TMH present; Function unclear.
 
 0.944
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.931
azo3626
Conserved hypothetical chaperon protein: Homology to cv2395 of C. violaceum of 62% (trembl|Q7NVE8). InterPro: Heat shock protein hsp70 (IPR001023). Pfam: Hsp70 protein. no signal peptide. no TMHs; Family membership.
  
 
 0.927
hscA
Probable chaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
  
 
 0.926
clpP
Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.
  
 
 0.925
sciC
Putative cytoplasmic protein, sciC, 42% identity (57% similarity) to TrEMBL; Q93IT3. Has PF05947, Bacterial protein of unknown function (DUF879);IPR010272; This family consists of several hypothetical bacterial proteins of unknown function; Function unclear.
 
  
 0.921
sciK
Putative cytoplasmic protein,sciK, 33% identity to TrEMBL;Q7AXZ0. Has PF05638, Protein of unknown function (DUF796);This family consists of several bacterial proteins of unknown function. Signal Peptide or TMH absent; Conserved hypothetical protein.
 
 
 0.915
azo1870
Endopeptidase Clp; Putative protease encoded ATP-dependent Clp protease family protein similar(30 Identity,45% similarity in function) to TrEMBL:Q8X866. IPR001907. Has pfam00574,CLP_protease, Clp protease. The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111,his-136 and asp-185 form the catalytic triad. One member has lost all of these active site residues and is therefore inactive. Some members contain one or two large insertions. Peptidase family S49 domain present. Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a [...]
   
 
 0.914
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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