STRINGSTRING
map protein (Acinetobacter baumannii) - STRING interaction network
"map" - Methionine aminopeptidase in Acinetobacter baumannii
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
mapMethionine aminopeptidase; Catalyzes the removal of N-terminal amino acids from peptides and arylamides; generally Co(II) however activity has been shown for some methionine aminopeptidases with Zn, Fe, or Mn; Derived by automated computational analysis using gene prediction method- Protein Homology (275 aa)    
Predicted Functional Partners:
rplC
50S ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3’-end of the 23S rRNA, where it nucleates assembly of the 50S subunit (212 aa)
 
 
  0.742
rplB
50S ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome (274 aa)
 
 
  0.738
rpsB
30S ribosomal protein S2; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the universal ribosomal protein uS2 family (250 aa)
 
 
  0.731
fusA
Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (712 aa)
 
 
  0.631
rpsI
30S ribosomal protein S9; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the universal ribosomal protein uS9 family (128 aa)
 
   
  0.616
AIL80288.1
Leucine--tRNA ligase; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family (874 aa)
 
 
  0.604
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 (878 aa)
 
   
  0.601
rplE
50S ribosomal protein L5; This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs (178 aa)
 
      0.596
rplD
50S ribosomal protein L4; Forms part of the polypeptide exit tunnel (200 aa)
 
 
  0.596
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)
   
   
  0.594
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
Server load: low (7%) [HD]