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
lepBSignal peptidase I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S26 family. (371 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.
  
 
 0.861
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.
  
  
 0.837
atpE
F0F1 ATP synthase subunit C; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
    
 0.751
OBX64754.1
DUF4845 domain-containing protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.672
ftsA
Cell division protein FtsA; Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. Belongs to the FtsA/MreB family.
 
 
   0.650
parC
DNA topoisomerase IV subunit A; Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule; Belongs to the type II topoisomerase GyrA/ParC subunit family. ParC type 1 subfamily.
  
    0.591
bamD
Transporter; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
  
  
 0.583
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.
  
    0.572
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.
   
    0.569
rseP
RIP metalloprotease RseP; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.550
Your Current Organism:
Moraxella lacunata
NCBI taxonomy Id: 477
Other names: ATCC 17967, Bacillus lacunatus, CCUG 4441, CIP A182, DSM 18052, Diplobacille de la conjonctivite subaigue, Diplobacillus moraxenfeld, JCM 20914, LMG 5301, LMG:5301, M. lacunata, NBRC 102154, NCTC 11011, strain Morax 260
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.