close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
pgpAPhosphatidylglycerophosphatase A; Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). (167 aa)    
Predicted Functional Partners:
pgsA
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase; Identified by similarity to SP:P06978; match to protein family HMM PF01066; match to protein family HMM TIGR00560; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
 
  
 0.945
MCA0372
Identified by similarity to GP:14027356; match to protein family HMM PF01066.
 
  
 0.939
ribBA
3,4-dihydroxy-2-butanone 4-phosphate synthase/GTP cyclohydrolase II; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; Belongs to the DHBP synthase family.
     
 0.857
thiL
Thiamine-monophosphate kinase; Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1; Belongs to the thiamine-monophosphate kinase family.
  
  
 0.842
nusB
N utilization substance protein B; Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
     
 0.810
ribE
6,7-dimethyl-8-ribityllumazine synthase; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin; Belongs to the DMRL synthase family.
     
 0.803
pstA
Phosphate ABC transporter, permease protein PstA; Identified by match to protein family HMM PF00528; match to protein family HMM TIGR00974.
      
 0.753
ribD
Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family.
     
 0.753
ribE-1
Riboflavin synthase, alpha subunit; Identified by similarity to SP:P51961; match to protein family HMM PF00677; match to protein family HMM TIGR00187.
       0.742
nrdR
Conserved hypothetical protein TIGR00244; Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR- boxes; Belongs to the NrdR family.
     
 0.683
Your Current Organism:
Methylococcus capsulatus
NCBI taxonomy Id: 243233
Other names: M. capsulatus str. Bath, Methylococcus capsulatus ATCC 33009, Methylococcus capsulatus Bath, Methylococcus capsulatus MC, Methylococcus capsulatus NCIB 11132, Methylococcus capsulatus str. Bath
Server load: low (36%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.