STRINGSTRING
hslO protein (Gallibacterium anatis) - STRING interaction network
"hslO" - Hsp33-like chaperonin in Gallibacterium anatis
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
hslOHsp33-like chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress (291 aa)    
Predicted Functional Partners:
nhaA
pH-dependent sodium/proton antiporter; Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons (397 aa)
              0.662
UMN179_01654
Ribosome-associated heat shock protein Hsp15 (135 aa)
   
        0.620
dusA
tRNA-dihydrouridine synthase A; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs (326 aa)
 
   
  0.571
glnE
Adenylyltransferase/deadenyltransferase; Adenylation and deadenylation of glutamate--ammonia ligase (968 aa)
   
          0.539
hslU
ATP-dependent protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis (444 aa)
     
   
  0.520
mltF
Putative transglycosylase; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella (486 aa)
 
          0.494
UMN179_02191
Hypothetical protein; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5’-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5’-phosphate (372 aa)
              0.491
UMN179_01847
Flavin mononucleotide phosphatase (236 aa)
   
 
    0.490
UMN179_01014
Nucleotidase (225 aa)
   
 
    0.490
rph
Ribonuclease PH; Phosphorolytic exoribonuclease that removes nucleotide residues following the -CCA terminus of tRNA and adds nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates (239 aa)
   
   
  0.488
Your Current Organism:
Gallibacterium anatis
NCBI taxonomy Id: 1005058
Other names: G. anatis, G. anatis UMN179, Gallibacterium, Gallibacterium Christensen et al. 2003 emend. Bisgaard et al. 2009, Gallibacterium anatis, Gallibacterium anatis UMN179, Gallibacterium anatis str. UMN179, Gallibacterium anatis strain UMN179, Pasteurella anatis, Salpingitia sp. 10672/6, Salpingitia sp. 10672/9, Salpingitia sp. 12158, Salpingitia sp. 20558, Salpingitia sp. 36961/sv7, Salpingitia sp. BJ3453, Salpingitia sp. BK3387.2, Salpingitia sp. CCM 5995, Salpingitia sp. Gerl.220, Salpingitia sp. Gerl.3348/80, Salpingitia sp. Gerl.4224, Salpingitia sp. IPDH 697/78, avian Pasteurella haemolytica complex
Server load: low (10%) [HD]