STRINGSTRING
feoA feoA feoB feoB feoC feoC bfd bfd exbB exbB exbD exbD yedY yedY fes fes insH1-2 insH1-2
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:
feoAFerrous iron transporter, protein A; Involved in Fe(2+) ion uptake. Does not stimulate the GTPase activity of the N-terminus of FeoB (residues 1- 276). (75 aa)
feoBFerrous iron transporter protein B and GTP-binding protein; Transporter of a GTP-driven Fe(2+) uptake system, probably couples GTP-binding to channel opening and Fe(2+) uptake. A guanine nucleotide-binding protein (G proteins) in which the guanine nucleotide binding site alternates between an active, GTP-bound state and an inactive, GDP- bound state. This protein has fast intrinsic GDP release, mediated by the G5 loop (about residues 149-158). Presumably GTP hydrolysis leads to conformational changes and channel closing. A GDP release mechanism involving a conformational change of the [...] (773 aa)
feoCPutative DNA-binding transcriptional regulator; May function as a transcriptional regulator that controls feoABC expression; Belongs to the FeoC family. (78 aa)
bfdBacterioferritin-associated ferredoxin; Seems to associate with BFR; could be a general redox and/or regulatory component participating in the iron storage mobilization functions of BFR. Could participate in the release or the delivery of iron from/to bacterioferritin (or other iron complexes). (64 aa)
exbBMembrane spanning protein in TonB-ExbB-ExbD complex; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB. (244 aa)
exbDMembrane spanning protein in TonB-ExbB-ExbD complex; Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. (141 aa)
yedYMembrane-anchored, periplasmic TMAO, DMSO reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The catalytic subunit Ms [...] (334 aa)
fesEnterobactin/ferrienterobactin esterase; Upon internalization, ferric enterobactin is processed via an exquisitely specific pathway that is dependent on FES activity, making iron available for metabolic use; Belongs to the Fes family. (400 aa)
insH1-2DLP12 prophage; truncated outer membrane porin (pseudogene);IS, phage, Tn; Phage or Prophage Related; outer membrane porin protein; locus of qsr prophage. (338 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
Server load: low (18%) [HD]