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:
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Cooccurrence
Coexpression
Experiments
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[Homology]
Score
Rv0968Conserved protein; Rv0968, (MTCY10D7.06c), len: 98 aa. Conserved protein, part of cso operon, similar to NP_301579.1|NC_002677 conserved hypothetical protein from Mycobacterium leprae (92 aa). Also highly similar to conserved hypothetical proteins from Mycobacterium tuberculosis e.g. Rv3269 (93 aa), FASTA score: (51.1% identity in 94 aa overlap); and Rv1993c (90 aa). (98 aa)    
Predicted Functional Partners:
ctpV
Probable metal cation transporter P-type ATPase CtpV; Necessary for copper homeostasis and likely functions as a copper exporter. Also required for full virulence.
  
  
 0.985
Rv0970
Rv0970, (MTCY10D7.04c), len: 210 aa. Probable conserved integral membrane protein, part of cso operon,equivalent to NP_302348.1|NC_002677 probable integral membrane protein from Mycobacterium leprae (210 aa).
  
  
 0.973
csoR
Copper-sensitive operon repressor CsoR; Copper-sensitive repressor that has a key role in copper homeostasis. It is part of the cso operon involved in the cellular response to increasing concentrations of copper inside the bacterium, which can be highly toxic. In the presence of copper, CsoR fully dissociates from the promoter in the cso operon, leading to the transcription of its genes. Binds to a GC-rich pseudopallindromic sequence, 5'-GTAGCCCACCCCCAGTGGGGTGGGA-3', in the cso promoter region.
  
  
 0.968
mmcO
Probable oxidase; Required for copper resistance. In vitro, oxidizes organic substrates and Fe(2+). May act in vivo by oxidation of toxic periplasmic Cu(+); Belongs to the multicopper oxidase family.
   
  
 0.547
Rv2963
Rv2963, (MTCY349.24c), len: 406 aa. Probable integral membrane protein.
  
  
 0.460
Rv0966c
Conserved protein; Rv0966c, (MTCY10D7.08), len: 200 aa. Conserved protein, equivalent to AL035500|MLCL373_12 conserved hypothetical protein from Mycobacterium leprae (200 aa),FASTA scores: opt: 1080, E(): 0, (79.5% identity in 200 aa overlap). Also highly similar to SCE6.30c|CAB88834.1|AL353832 hypothetical protein from Streptomyces coelicolor (277 aa). Some similarity to Rv2862c|MTV007.08 conserved hypothetical protein from Mycobacterium tuberculosis (194 aa), FASTA scores: E(): 3.1e-06, (31.5% identity in 184 aa overlap). Equivalent to AAK45243.1 from Mycobacterium tuberculosis strai [...]
       0.448
ricR
Conserved protein; Under low copper conditions, represses the expression of lpqS, Rv2963, mymT, socA, socB, mmcO and its own expression. In the presence of copper, RicR dissociates from DNA, leading to the expression of the target genes. Members of the RicR regulon are important for copper resistance during infections and full virulence in a mouse model of infection.
  
  
 0.440
Rv2952
Possible methyltransferase (methylase); Catalyzes the methylation of the lipid moiety of the intermediate compounds phthiotriol and glycosylated phenolphthiotriol dimycoserosates to form phthiocerol dimycocerosates (DIM A) and glycosylated phenolphthiocerol dimycocerosates (PGL). Belongs to the methyltransferase superfamily. Phthiotriol/phenolphthiotriol dimycocerosates methyltransferase family.
      
 0.433
mymT
Metallothionein, MymT; Metallothioneins are small proteins that have a high content of cysteine residues wich allow them to bind heavy metal ions through clusters of thiolate bonds. MymT binds up to seven ions of Cu(+), with a preference for four to six Cu(+) ions, in a solvent-shielded core. MymT protects M.tuberculosis from copper toxicity.
      
 0.431
lpqS
Probable lipoprotein LpqS; May play an essential role in M.tuberculosis replication and survival inside the host cell.
   
  
 0.429
Your Current Organism:
Mycobacterium tuberculosis H37Rv
NCBI taxonomy Id: 83332
Other names: M. tuberculosis H37Rv, Mycobacterium sp. H37Rv, Mycobacterium tuberculosis str. H37Rv, Mycobacterium tuberculosis strain H37Rv
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