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secY_1 protein (Bacillus cereus) - STRING interaction network
"secY_1" - Protein translocase subunit SecY in Bacillus cereus
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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secY_1Protein 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 (434 aa)    
Predicted Functional Partners:
secDF
Multifunctional fusion protein; 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 (754 aa)
 
  0.999
secA_1
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 (835 aa)
 
  0.993
secA_2
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 (788 aa)
 
  0.988
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) (329 aa)
 
  0.979
ffh
Signal recognition particle protein; 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; Belongs to the GTP-binding SRP family. SRP54 subfamily (449 aa)
 
  0.978
secG
secG- preprotein translocase, SecG subunit (77 aa)
     
  0.975
rpsM
30S ribosomal protein S13; Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P- sites (121 aa)
 
  0.968
rpsD
30S ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit (200 aa)
 
  0.967
rpsC
30S ribosomal protein S3; Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation (219 aa)
 
 
  0.955
rpsJ
30S ribosomal protein S10; Involved in the binding of tRNA to the ribosomes (102 aa)
 
 
  0.951
Your Current Organism:
Bacillus cereus
NCBI taxonomy Id: 1396
Other names: ATCC 14579, B. cereus, BCRC 10603, Bacillus cereus, Bacillus endorhythmos, Bacillus medusa, Bacillus sp. 2479, Bacillus sp. BS2(2013b), Bacillus sp. BV4, Bacillus sp. JKR50, Bacillus sp. JKR62, Bacillus sp. JP44SK22, Bacillus sp. JP44SK37, Bacillus sp. JP44SK43, Bacillus sp. JP44SK45, Bacillus sp. JSG1(2014), Bacillus sp. KER 17, Bacillus sp. MZ-01, Bacillus sp. PXDK-1, Bacillus sp. Pf-1, Bacillus sp. V3, Bacillus sp. mmm86, CCM 2010, CCRC 10603, CCUG 7414, CIP 66.24, DSM 31, IAM 12605, IFO 15305, JCM 2152, LMG 6923, NBRC 15305, NCCB 75008, NCIMB 9373, NCTC 2599, NRRL B-3711, VKM B-504
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