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
ssbSingle-strand binding protein; Identified by similarity to SP:P02339; match to protein family HMM PF00436; match to protein family HMM TIGR00621. (172 aa)    
Predicted Functional Partners:
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 [...]
  
 
 0.934
rpsF
Ribosomal protein S6; Binds together with S18 to 16S ribosomal RNA.
 
  
 0.880
dnaZX
DNA polymerase III, gamma and tau subunits; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
    
 
 0.860
priA
Primosomal protein N`; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily.
  
 
 
 0.853
dnaE
DNA polymerase III, alpha subunit; Identified by similarity to SP:P10443; match to protein family HMM PF01336; match to protein family HMM PF02231; match to protein family HMM PF02811; match to protein family HMM PF07733; match to protein family HMM TIGR00594.
 
 
 
 0.842
rpsB
Ribosomal protein S2; Identified by similarity to SP:P02351; match to protein family HMM PF00318; match to protein family HMM TIGR01011; Belongs to the universal ribosomal protein uS2 family.
  
   0.818
rplU
Ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family.
   
    0.813
dnaE2
Putative DNA polymerase III, alpha subunit; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase.
   
 
 0.809
dnaB
Replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins. Belongs to the helicase family. DnaB subfamily.
 
 
 0.807
MCA2098
Putative DNA polymerase III, chi subunit; Identified by similarity to SP:P28905; match to protein family HMM PF04364.
    
 
 0.805
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
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