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
AMG69391.1Hypothetical protein; OmpA is believed to be a porin, involved in diffusion of nonspecific small solutes across the outer membrane. It is the most abundant integral protein of the outer membrane of E. coli, and it is known to play a role as a phage receptor, a mediator of F-factor dependent conjugation, and in maintaining the structural shape of the outer membrane; 3a; II*; G; d; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the outer membrane OOP (TC 1.B.6) superfamily. (357 aa)    
Predicted Functional Partners:
skp
Molecular chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the skp family.
  
 
 0.940
secA
Preprotein translocase subunit SecA; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
   
 
 0.917
rplX
50S ribosomal protein L24; One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
  
 
 0.908
AMG71824.1
Biopolymer transporter Tol; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.897
rplW
50S ribosomal protein L23; One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome; Belongs to the universal ribosomal protein uL23 family.
   
 
 0.886
rpsN
30S ribosomal protein S14; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site; Belongs to the universal ribosomal protein uS14 family.
   
 
 0.881
rpsF
30S ribosomal protein S6; Binds together with S18 to 16S ribosomal RNA.
  
   0.872
AMG71084.1
Serine endoprotease DegQ; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S1C family.
   
 
 0.864
degS
Outer membrane-stress sensor serine endopeptidase DegS; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.864
rpsL
30S ribosomal protein S12; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
   
 
 0.863
Your Current Organism:
Morganella morganii
NCBI taxonomy Id: 582
Other names: ATCC 25830, ATCC 8076H, Bacillus morgani, CCUG 6328, CIP 103763, CIP A231, DSM 30164, IFO 3848, LMG 7874, LMG:7874, M. morganii, NBRC 3848, NCCB 73065, NCIB 235, NCIB:235, NCTC 235, Organism N 1, Proteus morganii, Salmonella morgani
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