STRINGSTRING
ACS38757.1 ACS38757.1 lolD lolD ACS40415.1 ACS40415.1 proS proS bamA bamA ACS42054.1 ACS42054.1 tolQ tolQ tolB tolB omp omp ACS39374.1 ACS39374.1 bamD bamD
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
ACS38757.1Putative Lipoprotein releasing system, transmembrane protein, LolC/E family; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. (439 aa)    
Predicted Functional Partners:
lolD
Outer membrane-specific lipoprotein transporter subunit; Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
 0.997
ACS40415.1
Putative transporter subunit: ATP-binding component of ABC superfamily; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter.
 
 
 0.925
proS
proline-tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro); Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 2 subfamily.
 
 
 
 0.830
bamA
Putative outer membrane protein assembly factor; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
 
   
 0.798
ACS42054.1
Conserved hypothetical protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).
   
 
 0.768
tolQ
Membrane spanning protein in TolA-TolQ-TolR complex; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
 
    0.761
tolB
Protein tolB precursor; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
  
  
 0.754
omp
Outer membrane lipoprotein omp16 precursor; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
  
 
 
 0.750
ACS39374.1
Membrane spanning protein in TonB-ExbB-ExbD complex; Function of strongly homologous gene; membrane component.
 
    0.747
bamD
Putative lipoprotein UPF0169; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
 
   
 0.707
Your Current Organism:
Methylorubrum extorquens
NCBI taxonomy Id: 272630
Other names: M. extorquens AM1, Methylobacterium extorquens AM1, Methylorubrum extorquens AM1, Pseudomonas sp. AM1
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.