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:
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
hisJHistidinol-phosphatase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the PHP hydrolase family. HisK subfamily (268 aa)    
Predicted Functional Partners:
hisD
Histidinol dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine
 
 
 0.976
hisC
Histidinol-phosphate aminotransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily
 
 
 0.975
polX
DNA polymerase/3'-5' exonuclease PolX; Strictly DNA-template-directed DNA polymerase, preferentially acting on DNA structures containing gaps from one to a few nucleotides and bearing a phosphate group at the 5' end of the downstream DNA. The fact that PolX is able to conduct filling of a single-nucleotide gap, allowing further sealing of the resulting nick by a DNA ligase, points to a putative role in base excision repair (BER) during the B.subtilis life cycle. Moreover, also possesses a 3'-5' exonuclease activity able to edit unpaired 3'-termini in a gapped DNA substrate and likely i [...]
     
 0.935
hisI
Histidine biosynthesis bifunctional protein HisIE; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; In the C-terminal section; belongs to the PRA-PH family
 
  
 0.874
hisB
Imidazoleglycerol-phosphate dehydratase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme
 
  
 0.873
hisG
ATP phosphoribosyltransferase; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity); Belongs to the ATP phosphoribosyltransferase family. Short subfamily
 
  
 0.776
yhaM
3'-5' exoribonuclease YhaM; Shows a 3'-5' exoribonuclease activity as well as single-stranded DNA 3'-5'exonuclease activity. Plays a role in the secondary pathway of 23S rRNA 3' end maturation; Belongs to the YhaM family
      
 0.761
hisF
Imidazole glycerol phosphate synthase subunit HisF; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (By similarity)
 
   
 0.711
ysnB
Putative metallophosphoesterase YsnB; Evidence 2b: Function of strongly homologous gene; Product type e: enzyme; Belongs to the metallophosphoesterase superfamily. YfcE family
  
  
 0.680
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
       0.657
Your Current Organism:
Bacillus subtilis
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis, Bacillus subtilis 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
Server load: low (6%) [HD]