STRINGSTRING
surA protein (Acinetobacter baumannii) - STRING interaction network
"surA" - Chaperone SurA in Acinetobacter baumannii
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
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 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 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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[Homology]
Score
surAChaperone SurA; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation (436 aa)    
Predicted Functional Partners:
AIL77515.1
LPS export ABC transporter periplasmic protein LptC; Derived by automated computational analysis using gene prediction method- Protein Homology (813 aa)
   
  0.959
AIL81119.1
Outer membrane protein assembly factor BamA; Derived by automated computational analysis using gene prediction method- Protein Homology (841 aa)
 
 
  0.816
AIL80273.1
Outer membrane protein assembly factor BamB; Derived by automated computational analysis using gene prediction method- Protein Homology (381 aa)
   
 
  0.799
bamD
Outer membrane protein assembly factor BamD; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane (385 aa)
   
 
  0.797
secB
Protein-export protein SecB; One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA (152 aa)
   
     
  0.764
AIL77514.1
Phosphotransferase; Derived by automated computational analysis using gene prediction method- Protein Homology (337 aa)
 
          0.721
AIL77513.1
Nucleotidyl transferase; Derived by automated computational analysis using gene prediction method- Protein Homology (229 aa)
   
        0.684
secA
Protein translocase subunit SecA; Functions in protein export; can interact with acidic membrane phospholipids and the SecYEG protein complex; binds to preproteins; binds to ATP and undergoes a conformational change to promote membrane insertion of SecA/bound preprotein; ATP hydrolysis appears to drive release of the preprotein from SecA and deinsertion of SecA from the membrane; additional proteins SecD/F/YajC aid SecA recycling; exists in an equilibrium between monomers and dimers; may possibly form higher order oligomers; proteins in this cluster correspond SecA1; SecA2 is not essen [...] (907 aa)
   
   
  0.682
dsbA
Thiol-disulfide interchange protein; Derived by automated computational analysis using gene prediction method- Protein Homology (205 aa)
   
 
  0.675
ksgA
Ribosomal RNA small subunit methyltransferase A; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3’-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits (270 aa)
 
   
  0.643
Your Current Organism:
Acinetobacter baumannii
NCBI taxonomy Id: 470
Other names: A. baumannii, ATCC 19606, Acinetobacter baumannii, Acinetobacter genomosp. 2, Acinetobacter genomospecies 2, Bacterium anitratum, CCUG 19096, CIP 70.34, DSM 30007, JCM 6841, NCCB 85021, NCTC 12156
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