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. (310 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.
0.999
secY
Preprotein translocase, SecY subunit; 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.
  
 
 0.889
ADQ05760.1
Membrane protein insertase, YidC/Oxa1 family; KEGG: ate:Athe_2760 60 kDa inner membrane insertion protein; TIGRFAM: membrane protein insertase, YidC/Oxa1 family; PFAM: 60 kDa inner membrane insertion protein.
   
 
 0.861
secE
Preprotein translocase, SecE subunit; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
  
 
 0.757
smc
Chromosome segregation protein SMC; Required for chromosome condensation and partitioning. Belongs to the SMC family.
  
    0.752
ADQ03850.1
KEGG: ate:Athe_0391 preprotein translocase, YajC subunit; TIGRFAM: preprotein translocase, YajC subunit; PFAM: YajC family protein.
  
  
 0.676
topA
DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...]
  
  
 0.660
ADQ04082.1
PFAM: Radical SAM domain protein; KEGG: ate:Athe_0623 radical SAM domain protein.
     
 0.621
ADQ04083.1
KEGG: ate:Athe_0624 carbonic anhydrase.
       0.592
rnj
RNA-metabolising metallo-beta-lactamase; An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.
  
    0.529
Your Current Organism:
Caldicellulosiruptor owensensis
NCBI taxonomy Id: 632518
Other names: C. owensensis OL, Caldicellulosiruptor owensensis DSM 13100, Caldicellulosiruptor owensensis OL, Caldicellulosiruptor owensensis str. OL, Caldicellulosiruptor owensensis strain OL
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