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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
secFProtein-export membrane protein SecF; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA; Belongs to the SecD/SecF family. SecF subfamily. (322 aa)    
Predicted Functional Partners:
secD
Protein-export membrane protein SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA; Belongs to the SecD/SecF family. SecD subfamily.
0.999
secY
Preprotein translocase subunit SecY; 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.
  
 0.970
EKF00192.1
Hypothetical protein; KEGG: ccs:CCNA_02444 0.54 N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase K01444; Psort location: CytoplasmicMembrane, score: 10.00.
  
 0.970
secE
Preprotein translocase subunit SecE; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
  
 0.934
EKF02202.1
Preprotein translocase, SecG subunit; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family.
    
 0.835
secA
Preprotein translocase, SecA subunit; 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.
  
 
 0.806
EKE98105.1
Hypothetical protein; KEGG: cno:NT01CX_2360 0.092 ribonuclease Z K00784; Psort location: Cytoplasmic, score: 8.96.
  
 
 0.695
EKE97100.1
Hypothetical protein; KEGG: tga:TGAM_0249 0.39 fdh1A; formate dehydrogenase I subunit A (fdh1A) K00123; Psort location: Cytoplasmic, score: 8.96.
  
 
 0.695
EKE96652.1
Plasmid protein; KEGG: rba:RB11313 5.0e-10 lexA; LexA repressor.
  
 
 0.695
EKF01874.1
Plasmid protein; KEGG: rba:RB11313 0.093 lexA; LexA repressor; Psort location: Cytoplasmic, score: 8.96.
  
 
 0.695
Your Current Organism:
Tolypothrix sp. PCC7601
NCBI taxonomy Id: 1188
Other names: Calothrix sp. PCC 7601, Fremyella diplosiphon ACMM 396, Fremyella diplosiphon IAM M-100, Fremyella diplosiphon UTEX B 481, Microchaete diplosiphon UTEX B 481, T. sp. PCC 7601, Tolypothrix (Calothrix) sp. PCC 7601, Tolypothrix sp. PCC 7601, Tolypothrix sp. PCC 7601 = UTEX B 481
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.