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
hypEHypothetical protein; KEGG: tep:TepRe1_0239 2.7e-55 Thiamine-phosphate kinase; Psort location: Cytoplasmic, score: 7.50. (348 aa)    
Predicted Functional Partners:
KXA30368.1
Prepilin-type cleavage/methylation protein.
  
    0.780
outO
Bacterial peptidase A24 protein; KEGG: clj:CLJU_c05610 7.7e-35 bifunctional type IV leader peptidase/N-methyltransferase; K02654 leader peptidase (prepilin peptidase) / N-methyltransferase; Psort location: CytoplasmicMembrane, score: 10.00.
       0.780
KXA30370.1
Hypothetical protein; KEGG: fnu:FN0522 8.5e-07 exonuclease SbcC K03546; Psort location: Cytoplasmic, score: 7.50.
       0.773
epsF
Bacterial type II secretion system protein F domain protein; KEGG: pfe:PSF113_5005 5.4e-27 pilC; protein PilC K02653; Psort location: CytoplasmicMembrane, score: 10.00.
       0.769
porA
KEGG: fma:FMG_0385 0. pyruvate/ferredoxin oxidoreductase; K03737 putative pyruvate-flavodoxin oxidoreductase; Psort location: Cytoplasmic, score: 7.50.
 
   
 0.683
rph
tRNA nucleotidyltransferase; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
       0.600
KXA30374.1
Non-canonical purine NTP pyrophosphatase, RdgB/HAM1 family; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.
       0.600
lytC
KEGG: ccl:Clocl_1228 6.3e-45 N-acetylmuramoyl-L-alanine amidase; K01448 N-acetylmuramoyl-L-alanine amidase; Psort location: Cellwall, score: 8.28.
       0.584
topA
DNA topoisomerase I; 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 DNA supe [...]
       0.532
epsE
KEGG: pen:PSEEN2333 5.7e-87 XcpR-2; type II secretion pathway protein E K02454; Psort location: Cytoplasmic, score: 9.97.
       0.532
Your Current Organism:
Peptoniphilus harei
NCBI taxonomy Id: 54005
Other names: ATCC BAA-601, CCUG 38491, CIP 105323, DSM 10020, NCTC 13076, P. harei, Peptostreptococcus harei, Schleiferella harei
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