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ftsH protein (Dermacoccus nishinomiyaensis) - STRING interaction network
"ftsH" - ATP-dependent zinc metalloprotease FtsH in Dermacoccus nishinomiyaensis
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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ftsHATP-dependent zinc metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family (682 aa)    
Predicted Functional Partners:
HX89_12580
7,8-dihydroneopterin aldolase; Catalyzes the conversion of 7,8-dihydroneopterin to 6- hydroxymethyl-7,8-dihydropterin (323 aa)
   
   
  0.937
HX89_12585
Dihydropteroate synthase; Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives (327 aa)
 
   
  0.903
folE
GTP cyclohydrolase 1; Derived by automated computational analysis using gene prediction method- Protein Homology (197 aa)
   
   
  0.898
HX89_12575
Uncharacterized protein; Derived by automated computational analysis using gene prediction method- Protein Homology (177 aa)
   
        0.861
dnaK
Chaperone protein DnaK; Acts as a chaperone (628 aa)
 
 
  0.791
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 (538 aa)
 
   
  0.773
atpA
ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit (544 aa)
   
 
  0.761
alaS
Alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction- alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain (904 aa)
 
   
  0.758
lepA
Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner (613 aa)
 
 
  0.755
HX89_02175
Phosphate acetyltransferase; Involved in acetate metabolism; In the N-terminal section; belongs to the CobB/CobQ family (691 aa)
         
  0.728
Your Current Organism:
Dermacoccus nishinomiyaensis
NCBI taxonomy Id: 1274
Other names: ATCC 29093, CCM 2140, CCUG 33028, CIP 81.71, D. nishinomiyaensis, DSM 20448, Dermacoccus nishinomiyaensis, Dermacoccus nishinomiyensis, Dermatococcus nishinomiyaensis, Dermatococcus nishinomiyensis, IEGM 393, IFO 15356, JCM 11613, LMG 14222, Micrococcus nishinomiyaensis, Micrococcus nishinomyaensis, NBRC 15356, NCTC 11039
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