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JG24_18975 protein (Klebsiella pneumoniae) - STRING interaction network
"JG24_18975" - Signal peptidase I in Klebsiella pneumoniae
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
JG24_18975Signal peptidase I; Catalyzes the cleavage of the amino-terminal leader peptide from secretory proteins; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the peptidase S26 family (324 aa)    
Predicted Functional Partners:
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 (599 aa)
 
   
  0.954
yidC
Membrane protein insertase YidC; Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins (548 aa)
 
 
  0.830
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 (443 aa)
   
   
  0.815
gltB
Glutamate synthase [NADPH] large chain; Catalyzes the formation of glutamate from glutamine and alpha-ketoglutarate; Derived by automated computational analysis using gene prediction method- Protein Homology (1486 aa)
   
   
  0.736
rnc
Ribonuclease 3; Digests double-stranded RNA (226 aa)
   
  0.713
yajC
Member of preprotein translocase; forms a heterotrimer with SecD and SecF; links the SecD/SecF/YajC/YidC complex with the SecY/SecE/SecG complex; Derived by automated computational analysis using gene prediction method- Protein Homology (110 aa)
 
   
  0.683
JG24_27270
Part of a complex with YfgL, YfiO, and NlpB involved in outer membrane protein biosynthesis; involved in the assembly of outer membrane proteins; Derived by automated computational analysis using gene prediction method- Protein Homology (807 aa)
 
 
  0.662
rpoH
RNA polymerase sigma factor RpoH; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes (284 aa)
 
   
  0.656
lspA
Lipoprotein signal peptidase; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family (166 aa)
 
   
  0.648
secG
Preprotein translocase subunit SecG (TC 3.A.5.1.1); Derived by automated computational analysis using gene prediction method- Protein Homology (109 aa)
 
     
  0.645
Your Current Organism:
Klebsiella pneumoniae
NCBI taxonomy Id: 573
Other names: ATCC 13883, Bacillus pneumoniae, Bacterium pneumoniae crouposae, CCUG 225, CIP 82.91, DSM 30104, HAMBI 450, Hyalococcus pneumoniae, IFO 14940, K. pneumoniae, Klebsiella pneumoniae, Klebsiella sp. M-AI-2, Klebsiella sp. PB12, Klebsiella sp. RCE-7, LMG 2095, NBRC 14940, NCTC 9633
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