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
rseCPfam:pfam04246 Positive regulator of sigma(E), RseC/MucC. (149 aa)    
Predicted Functional Partners:
rseB
Anti sigma E (Sigma 24) factor, negative regulator; Pfam:pfam03888 MucB/RseB family.
 
  
 0.992
rseA
Anti-sigma-E factor RseA; An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic proteases finish de [...]
 
  
 0.956
rpoE-4
RNA polymerase sigma-70 factor, ECF subfamily; Pfam:pfam04542 Sigma-70 region 2; Belongs to the sigma-70 factor family. ECF subfamily.
  
  
 0.899
nadB
L-aspartate oxidase; Catalyzes the oxidation of L-aspartate to iminoaspartate.
 
     0.815
recO
DNA repair protein RecO; Involved in DNA repair and RecF pathway recombination.
 
     0.814
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.
       0.793
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.
       0.785
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.
       0.785
lepB-2
Pfam:pfam00717 Peptidase S24-like; Belongs to the peptidase S26 family.
       0.785
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.
       0.758
Your Current Organism:
Pseudoalteromonas issachenkonii
NCBI taxonomy Id: 152297
Other names: CIP 106858, DSM 15925, KCTC 12958, KMM 3549, LMG 19697, LMG:19697, P. issachenkonii, Pseudoalteromonas issachenkonii Ivanova et al. 2002, Pseudoalteromonas sp. F13, Pseudoalteromonas sp. F2, Pseudoalteromonas sp. KMM 3549
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.