STRING allows inspection of the interaction evidence for any given network. Choose any of the viewers above (disabled if not applicable in your network).
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.
colored nodes: query proteins and first shell of interactors
white nodes: second shell of interactors
empty nodes: proteins of unknown 3D structure
filled nodes: some 3D structure is known or predicted
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 each other.
from curated databases
SSU ribosomal protein S18P alanine acetyltransferase (153 aa)
Predicted Functional Partners:
Peptidase M22, glycoprotease (231 aa)
DNA-binding/iron metalloprotein/AP endonuclease; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction (339 aa)
Helicase c2 (646 aa)
Phage SPO1 DNA polymerase-related protein (330 aa)
Integron integrase (334 aa)
Cation efflux protein (204 aa)
YjeF-related protein-like protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (487 aa)
prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction- proline is first activated by ATP to form Pro- AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as ’pretransfer’ editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated ’posttransfer’ editing and involves dea [...] (573 aa)
PTS system fructose subfamily IIA component (136 aa)
GCN5-related N-acetyltransferase (153 aa)
Your Current Organism:
NCBI taxonomy Id: 265072 Other names: M. flagellatus, M. flagellatus KT, Methylobacillus, Methylobacillus flagellatus, Methylobacillus flagellatus KT, Methylobacillus flagellatus str. KT, Methylobacillus flagellatus strain KT