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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
hflBCell division protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. (645 aa)    
Predicted Functional Partners:
hflK
Putative phage-related protein; HflC and HflK could encode or regulate a protease.
  
 0.956
hflC
Putative phage-related protein; HflC and HflK could regulate a protease.
  
 0.930
rrmJ
Ribosomal RNA large subunit methyltransferase; Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
 
  
 0.926
secY
Preprotein translocase subunit; 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.
  
 
 0.866
htpX
Heat shock protein; Similar to Escherichia coli probable protease HtpX or b1829 SWALL:HTPX_ECOLI (SWALL:P23894) (293 aa) fasta scores: E(): 1.5e-100, 89.76% id in 293 aa; Belongs to the peptidase M48B family.
  
 0.853
rpsA
30S ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence.
  
   0.850
hpt
Similar to Salmonella typhimurium hypoxanthine phosphoribosyltransferase Hpt or stm0170 SWALL:HPRT_SALTY (SWALL:O33799) (178 aa) fasta scores: E(): 1.2e-54, 86.2% id in 174 aa, and to Escherichia coli, Escherichia coli O6, and Shigella flexneri hypoxanthine phosphoribosyltransferase Hpt or b0125 or c0154 or sf0122 SWALL:HPRT_ECOLI (SWALL:P36766) (178 aa) fasta scores: E(): 2.4e-54, 84.48% id in 174 aa; Belongs to the purine/pyrimidine phosphoribosyltransferase family.
  
  
 0.835
rpsK
30S ribosomal subunit protein S11; Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome; Belongs to the universal ribosomal protein uS11 family.
  
 
 0.834
atpA
ATP synthase alpha chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.
   
 0.829
clpX
ATP-dependent Clp protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
  
  
 0.816
Your Current Organism:
Pectobacterium atrosepticum
NCBI taxonomy Id: 218491
Other names: Erwinia carotovora subsp. atroseptica SCRI1043, Erwinia carotovora subsp. atroseptica str. SCRI1043, P. atrosepticum SCRI1043, Pectobacterium atrosepticum SCRI1043, Pectobacterium atrosepticum str. SCRI1043, Pectobacterium atrosepticum strain SCRI1043, Pectobacterium carotovora subsp. atroseptica SCRI1043, Pectobacterium carotovora subsp. atroseptica str. SCRI1043
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