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
greAPutative transcription elongation factor; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. (162 aa)    
Predicted Functional Partners:
rpoC
DNA-directed RNA polymerase beta' chain; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
 
 0.995
rpoB
DNA-directed RNA polymerase beta chain; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
   
 
 0.990
rpoA
DNA-directed RNA polymerase alpha chain; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
 
 
 0.972
rpoZ
Putative DNA-directed RNA polymerase omega chain; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
 
 
 
 0.960
CMS2431
Putative membrane protein.
       0.693
nusG
Transcription antitermination protein; Participates in transcription elongation, termination and antitermination.
 
  
 0.687
mfd
Transcription-repair coupling factor; Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site; In the C-terminal section; belongs to the helicase family. RecG subfamily.
     
 0.649
mca
Conserved hypothetical protein; A mycothiol (MSH, N-acetylcysteinyl-glucosaminyl-inositol) S- conjugate amidase, it recycles conjugated MSH to the N-acetyl cysteine conjugate (AcCys S-conjugate, a mercapturic acid) and the MSH precursor. Involved in MSH-dependent detoxification of a number of alkylating agents and antibiotics; Belongs to the MshB deacetylase family. Mca subfamily.
 
     0.626
nusB
Transcription termination protein; 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.
 
  
 0.602
CMS2429
Putative membrane protein.
       0.578
Your Current Organism:
Clavibacter michiganensis sepedonicus
NCBI taxonomy Id: 31964
Other names: ATCC 33113, Aplanobacter sepedonicum, Bacterium sepedonicum, C. michiganensis subsp. sepedonicus, CCUG 23908, CFBP 2049, CIP 104844, Clavibacter michiganense sepedonicum, Clavibacter michiganensis sepedonicum, Clavibacter michiganensis subsp. sepedonicus, Clavibacter sepedonicus nom. illegit., Corynebacterium michiganense subsp. sepedonicum, Corynebacterium sepedonicum, DSM 20744, ICMP 2535, JCM 9667, LMG 2889, LMG:2889, Mycobacterium sepedonicum, NCPPB 2137, Phytomonas sepedonica, Pseudobacterium sepedonicum
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