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
ADW17220.1Signal recognition particle-docking protein FtsY; COGs: COG0552 Signal recognition particle GTPase; InterPro IPR003593: IPR013822: IPR000897: IPR004390; KEGG: dps:DP2936 cell division protein FtsY; PFAM: GTP-binding signal recognition particle SRP54 G- domain; GTP-binding signal recognition particle SRP54 helical bundle; SMART: AAA ATPase; SPTR: Cell division transporter substrate-binding protein FtsY; TIGRFAM: signal recognition particle-docking protein FtsY; PFAM: SRP54-type protein, GTPase domain; SRP54-type protein, helical bundle domain; TIGRFAM: signal recognition particle-dockin [...] (592 aa)    
Predicted Functional Partners:
ffh
Signal recognition particle subunit FFH/SRP54 (srp54); Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the i [...]
 
0.997
secY
Protein translocase subunit secY/sec61 alpha; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
   
 0.991
ADW17815.1
Gliding motility protein (MglA); COGs: COG2229 GTPase; InterPro IPR001806; KEGG: dps:DP2776 gliding motility protein (MglA); SPTR: Probable gliding motility protein (MglA); PFAM: Ras family; TIGRFAM: small GTP-binding protein domain.
   
 0.985
ADW19276.1
COGs: COG1314 Preprotein translocase subunit SecG; InterPro IPR004692; KEGG: dak:DaAHT2_0038 preprotein translocase, SecG subunit; PFAM: Preprotein translocase SecG subunit; SPTR: Preprotein translocase, SecG subunit; TIGRFAM: preprotein translocase, SecG subunit; PFAM: Preprotein translocase SecG subunit; TIGRFAM: protein translocase, SecG subunit.
   
 0.981
ADW16952.1
Preprotein translocase, SecE subunit; InterPro IPR001901: IPR005807; KEGG: dps:DP1111 preprotein translocase SecE subunit (partial length); PFAM: protein secE/sec61-gamma protein; SPTR: Related to preprotein translocase secE subunit (Partial length); TIGRFAM: preprotein translocase, SecE subunit; manually curated; PFAM: SecE/Sec61-gamma subunits of protein translocation complex; TIGRFAM: preprotein translocase, SecE subunit, bacterial.
    
 0.979
ADW19084.1
COGs: COG0342 Preprotein translocase subunit SecD; InterPro IPR003335: IPR005791: IPR005665; KEGG: dps:DP0806 protein-export membrane protein SecD; PFAM: SecD/SecF/SecDF export membrane protein; SPTR: Related to protein-export membrane protein SecD; TIGRFAM: protein-export membrane protein SecD; protein-export membrane protein, SecD/SecF family; protein-export membrane protein SecF; PFAM: Protein export membrane protein; SecD/SecF GG Motif; TIGRFAM: protein-export membrane protein SecD; protein-export membrane protein, SecD/SecF family; protein-export membrane protein SecF.
    
 0.962
ADW16216.1
COGs: COG1862 Preprotein translocase subunit YajC; InterPro IPR003849; KEGG: dak:DaAHT2_1913 preprotein translocase, YajC subunit; PFAM: YajC family protein; SPTR: Preprotein translocase, YajC subunit; TIGRFAM: preprotein translocase, YajC subunit; PFAM: Preprotein translocase subunit; TIGRFAM: preprotein translocase, YajC subunit.
 
  
 0.942
ADW16967.1
COGs: COG0089 Ribosomal protein L23; InterPro IPR013025; KEGG: dps:DP1126 50S ribosomal protein L23; PFAM: Ribosomal protein L25/L23; SPTR: 50S ribosomal protein L23; PFAM: Ribosomal protein L23.
  
 
 0.941
secA
Protein 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 as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family.
  
  
 0.939
ADW16980.1
COGs: COG0200 Ribosomal protein L15; InterPro IPR005749: IPR001196; KEGG: dps:DP1144 50S ribosomal protein L15; SPTR: 50S ribosomal protein L15; TIGRFAM: ribosomal protein L15; manually curated; PFAM: Ribosomal protein L18e/L15; TIGRFAM: ribosomal protein L15, bacterial/organelle.
  
 
 0.935
Your Current Organism:
Desulfobulbus propionicus
NCBI taxonomy Id: 577650
Other names: D. propionicus DSM 2032, Desulfobulbus propionicus DSM 2032, Desulfobulbus propionicus str. DSM 2032, Desulfobulbus propionicus strain DSM 2032
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.