STRINGSTRING
STRING protein interaction network
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:
a 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 to 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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
HA50_14670S26 family signal peptidase; 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. (323 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.
  
 
 0.981
minE
Cell division topological specificity factor MinE; Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
   
    0.972
HA50_02390
RNA polymerase factor sigma-54; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.
  
  
 0.940
lolB
Lipoprotein localization factor LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
   
  
 0.939
HA50_11175
Protease; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.929
bamD
Outer membrane protein assembly factor BamD; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamA, the core component of the assembly machinery.
 
  
 0.905
HA50_11185
Murein DD-endopeptidase MepM; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.863
rnc
Ribonuclease III; 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.
  
  
 0.853
tuf-2
Translation elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.
   
  
 0.851
HA50_06855
Porin OmpA; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the outer membrane OOP (TC 1.B.6) superfamily.
 
  
 0.821
Your Current Organism:
Pantoea cypripedii
NCBI taxonomy Id: 55209
Other names: ATCC 29267, Bacillus cypripedii, CFBP 3613, CIP 105195, DSM 3873, Erwinia carotovora var. cypripedii, Erwinia cypripedii, Erwinia cyrpipedii, LMG 2655, LMG 2657, LMG:2655, LMG:2657, NCPPB 3004, P. cypripedii, Pectobacterium cypripedii
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