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secA protein (Pseudoflavonifractor capillosus) - STRING interaction network
"secA" - Protein translocase subunit SecA in Pseudoflavonifractor capillosus
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secAProtein 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 (919 aa)    
Predicted Functional Partners:
secY
Protein 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 (453 aa)
 
 
  0.991
rpoD
RNA polymerase sigma factor SigA ; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth (441 aa)
 
 
  0.910
ftsZ
Cell division protein FtsZ ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity (379 aa)
 
 
  0.827
tsaD
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD ; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction (345 aa)
 
   
  0.801
BACCAP_03461
Alkaline phosphatase family protein (526 aa)
       
 
  0.797
secE
Preprotein translocase, SecE subunit (103 aa)
       
 
  0.748
tig
PPIase ; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (464 aa)
 
   
  0.747
ftsY
Signal recognition particle receptor FtsY ; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC) (299 aa)
   
 
  0.728
frr
Ribosome-releasing factor ; Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another (184 aa)
 
   
  0.716
ffh
Fifty-four homolog ; 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 (456 aa)
   
 
  0.697
Your Current Organism:
Pseudoflavonifractor capillosus
NCBI taxonomy Id: 411467
Other names: Bacillus capillosus, Bacteroides capillosus, Bacteroides capillosus ATCC 29799, P. capillosus, P. capillosus ATCC 29799, Pseudobacterium capillosum, Pseudoflavonifractor, Pseudoflavonifractor Carlier et al. 2010, Pseudoflavonifractor capillosus, Pseudoflavonifractor capillosus ATCC 29799, Pseudoflavonifractor capillosus str. ATCC 29799, Pseudoflavonifractor capillosus strain ATCC 29799, Ristella capillosa
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