STRINGSTRING
secF secF secA secA Rta_26440 Rta_26440 secD secD
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:
secFCandidate preprotein translocase, subunit SecF; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. (317 aa)
secACandidate preprotein translocase SecA subunit; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. Belongs to the SecA family. (926 aa)
Rta_26440Candidate preprotein translocase, subunit SecG; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family. (145 aa)
secDCandidate preprotein translocase, subunit SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. (616 aa)
Your Current Organism:
Ramlibacter tataouinensis
NCBI taxonomy Id: 365046
Other names: Acidivorax sp. TTB310, Acidovorax sp. TTB310, R. tataouinensis TTB310, Ramlibacter tataouinensis TTB310, Ramlibacter tataouinensis str. TTB310, Ramlibacter tataouinensis strain TTB310
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