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
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
Slit_0104Phosphotransferase system, phosphocarrier protein HPr; KEGG: mfa:Mfla_0147 HPrNtr; TIGRFAM: phosphocarrier, HPr family; PFAM: phosphoryl transfer system HPr. (89 aa)    
Predicted Functional Partners:
Slit_0105
Phosphoenolpyruvate-protein phosphotransferase; General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
 
 0.999
Slit_0103
PFAM: PTS system fructose subfamily IIA component; KEGG: mmb:Mmol_2160 PTS system fructose subfamily IIA component.
 
 
 0.995
hprK
HPr kinase; Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr).
 
 
 
 0.871
Slit_0434
Putative PTS IIA-like nitrogen-regulatory protein PtsN; PFAM: phosphoenolpyruvate-dependent sugar phosphotransferase system EIIA 2; KEGG: neu:NE0060 phosphotransferase system mannitol/fructose-specific IIA domain-containing protein.
 
  
 0.850
Slit_0100
KEGG: tbd:Tbd_2408 glutamate--cysteine ligase GshA; TIGRFAM: glutamate/cysteine ligase; PFAM: glutamate--cysteine ligase GshA.
     
 0.795
Slit_0101
ApbE family lipoprotein; Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein. Belongs to the ApbE family.
       0.791
Slit_0102
Hypothetical protein; KEGG: solute carrier family 37 member 2 (glycerol-3-phosphate transporter.
       0.773
rpsG
Ribosomal protein S7; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family.
  
    0.557
Slit_2266
KEGG: eba:ebA6177 hypothetical protein.
    
 
 0.533
rpsL
Ribosomal protein S12; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
  
    0.512
Your Current Organism:
Sideroxydans lithotrophicus
NCBI taxonomy Id: 580332
Other names: S. lithotrophicus ES-1, Sideroxydans lithotrophicus ES-1, Sideroxydans lithotrophicus str. ES-1, Sideroxydans lithotrophicus strain ES-1, iron-oxidizing lithotroph ES-1
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