STRINGSTRING
cusA cusA ompF ompF ompC ompC ompR ompR mutM mutM mutL mutL tamB tamB cusS cusS cusC cusC cusR cusR cusF cusF cusB cusB
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
Your Input:
cusACopper/silver efflux system, membrane component; Part of a cation efflux system that mediates resistance to copper and silver; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. (1047 aa)
ompFOuter membrane porin 1a (Ia;b;F); Forms pores that allow passive diffusion of small molecules across the outer membrane. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity; Belongs to the Gram-negative porin family. (362 aa)
ompCOuter membrane porin protein C; Forms pores that allow passive diffusion of small molecules across the outer membrane. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity; Belongs to the Gram-negative porin family. (367 aa)
ompRResponse regulator in two-component regulatory system with EnvZ; Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes. Plays a central role in both acid and osmotic stress responses. Binds to the promoter of both ompC and ompF; at low osmolarity it activates ompF transcription, while at high osmolarity it represses ompF and activates ompC transcription. Involved in acid stress response; this requires EnvZ but not OmpR phosphorylation. Phosphorylated by EnvZ; this stimulates OmpR's DNA-binding abi [...] (239 aa)
mutMFormamidopyrimidine/5-formyluracil/ 5-hydroxymethyluracil DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) and its derivatives such as guanidinohydantoin:C and spiroiminodihydantoin:C, however it also acts on thymine glycol:G, 5,6-dihydrouracil:G and 5-hydroxyuracil:G. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-de [...] (269 aa)
mutLMethyl-directed mismatch repair protein; This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of the final effector complex. The ATPase activity of MutL is stimulated by DNA. (615 aa)
tamBTranslocation and assembly module for autotransporter export, inner membrane subunit; Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane. In reconstituted TAM this subunit (Ag43, AC P39180) is not necessary for substrate penetration in the outer membrane. Substrate binding to TamA moves its POTRA domains about 30 Angstroms into the periplasm, which would deform either the outer membrane or TamB and may provide force to reset TAM. (1259 aa)
cusSCopper-sensing histidine kinase in two-component regulatory system with CusR; Member of the two-component regulatory system CusS/CusR involved in response to copper and silver. Acts as a copper/silver ion sensor. Activates CusR by phosphorylation. (480 aa)
cusCCopper/silver efflux system, outer membrane component; Forms pores that allow passive diffusion of cations across the outer membrane. Part of a cation efflux system that mediates resistance to copper and silver. In pathogenic strains it allows the bacteria to invade brain microvascular endothelial cells (BMEC) thus allowing it to cross the blood-brain barrier and cause neonatal meningitis. (457 aa)
cusRResponse regulator in two-component regulatory system with CusS; Member of the two-component regulatory system CusS/CusR involved in response to copper and silver. Activates the expression of cusCFBA, hiuH and plasmid pRJ1004 gene pcoE in response to increasing levels of copper or silver ions. Can also increase the basal-level expression of copper resistance gene operon pcoABCD. (227 aa)
cusFPeriplasmic copper- and silver-binding protein; Part of a cation efflux system that mediates resistance to copper and silver. Binds one copper per polypeptide. (110 aa)
cusBCopper/silver efflux system, membrane fusion protein; Part of a cation efflux system that mediates resistance to copper and silver. (407 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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