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
Databases
Textmining
[Homology]
Score
zntACation-transporting ATPase, P-type; Similar to GB:AE000782 percent identity: 38.53; identified by sequence similarity; putative. (792 aa)    
Predicted Functional Partners:
TP_0939
Pyruvate oxidoreductase; Similar to PID:1001780 SP:P52965 PID:1006618 percent identity: 58.44; identified by sequence similarity; putative.
  
  
 0.790
mgtC
Mg2+ transport protein (mgtC); Similar to PID:1001492 PID:1001567 percent identity: 48.39; identified by sequence similarity; putative.
     
 0.723
murJ
Virulence factor (mviN); Involved in peptidoglycan biosynthesis. Transports lipid- linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
      
 0.666
valS
valyl-tRNA synthetase (valS); 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.
     
 0.591
secA
Preprotein translocase subunit (secA); Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane; Belongs to the SecA family.
 
   
 0.547
msrAB
protein-methionine-S-oxide reductase (msrA); Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
  
  
 0.521
macA
Membrane fusion protein, putative; Similar to GB:L42023 PID:1005989 PID:1220998 PID:1205141 SP:Q57500 percent identity: 25.88; identified by sequence similarity; putative.
  
  
 0.514
topA
DNA topoisomerase I (topA); Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing D [...]
     
 0.484
rpmE
Ribosomal protein L31 (rpmE); Binds the 23S rRNA.
     
 0.473
pgk
Phosphoglycerate kinase (pgk); Similar to GB:L32595 PID:483399 SP:Q59181 PID:1314258 GB:AE000783 percent identity: 48.99; identified by sequence similarity; putative; Belongs to the phosphoglycerate kinase family.
      0.469
Your Current Organism:
Treponema pallidum
NCBI taxonomy Id: 243276
Other names: T. pallidum subsp. pallidum str. Nichols, Treponema pallidum Nichols, Treponema pallidum subsp. pallidum str. Nichols
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