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
msrCFree methionine-R-sulfoxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (151 aa)    
Predicted Functional Partners:
AJC97086.1
Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase protein; Catalyzes the formation of 5,10-methylenetetrahydrofolate from 5-methyltetrahydrofolate and S-adenosyl-L-homocysteine and methionine from S-adenosyl-L-methionine and L-homocysteine; expressed in B. subtilis under methionine starvation conditions; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.901
AJC95425.1
N-succinyldiaminopimelate aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.900
metK
S-adenosylmethionine synthetase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
     
  0.900
metE
5-methyltetrahydropteroyltriglutamate-- homocysteine methyltransferase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation; Belongs to the vitamin-B12 independent methionine synthase family.
     
  0.900
valS
valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
     
 0.748
AJC95949.1
Aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.706
thiI
Putative tRNA sulfurtransferase; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
       0.706
AJC95951.1
Membrane protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.697
ezrA
Septation ring formation regulator EzrA; Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization; Belongs to the EzrA family.
       0.546
rpsD
30S ribosomal protein S4; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
       0.493
Your Current Organism:
Staphylococcus hyicus
NCBI taxonomy Id: 1284
Other names: ATCC 11249, CCM 2368, CCUG 6509, CIP 81.58, DSM 20459, JCM 2423, LMG 13352, LMG:13352, Micrococcus hyicus, NCTC 10350, S. hyicus, Staphylococcus hyicus hyicus, Staphylococcus hyicus subsp. hyicus
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