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lepB protein (Acinetobacter baumannii) - STRING interaction network
"lepB" - Signal peptidase I in Acinetobacter baumannii
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query proteins and first shell of interactors
white nodes:
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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Gene Fusion
Cooccurence
Coexpression
Experiments
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Textmining
[Homology]
Score
lepBSignal peptidase I; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the peptidase S26 family (275 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 (605 aa)
 
   
  0.935
rnc
Ribonuclease 3; Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre- crRNA and tracrRNA of type II CRISPR loci if present in the organism (230 aa)
 
   
  0.895
ABUW_1031
DUF4845 domain-containing protein; Derived by automated computational analysis using gene prediction method- Protein Homology (124 aa)
   
        0.876
era
GTPase Era; An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism (342 aa)
        0.868
pdxJ
Pyridoxine 5’-phosphate synthase; Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5’-phosphate (PNP) and inorganic phosphate (241 aa)
     
  0.833
lspA
Lipoprotein signal peptidase; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family (176 aa)
 
   
  0.803
recO
DNA repair protein RecO; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the RecO family (237 aa)
   
        0.794
AB895_0528
Uncharacterized protein; Derived by automated computational analysis using gene prediction method- Protein Homology (66 aa)
              0.734
ABUW_1037
Putative tRNA-(Ms(2)io(6)a)-hydroxylase; Derived by automated computational analysis using gene prediction method- Protein Homology (214 aa)
              0.718
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 (450 aa)
   
   
  0.714
Your Current Organism:
Acinetobacter baumannii
NCBI taxonomy Id: 470
Other names: A. baumannii, ATCC 19606, Acinetobacter baumannii, Acinetobacter genomosp. 2, Acinetobacter genomospecies 2, Bacterium anitratum, CCUG 19096, CIP 70.34, DSM 30007, JCM 6841, NCCB 85021, NCTC 12156
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