STRINGSTRING
tatC tatC secA secA secF secF secD secD AOK53329.1 AOK53329.1 AOK56621.1 AOK56621.1 secE secE AOK51324.1 AOK51324.1 secY secY tatA tatA tatB tatB
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:
tatCTwin-arginine protein translocation system subunit TatC; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides. (260 aa)
secAPreprotein translocase subunit SecA; 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. (933 aa)
secFPreprotein 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. (316 aa)
secDPreprotein 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. (671 aa)
AOK53329.1Preprotein translocase subunit SecG; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family. (125 aa)
AOK56621.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (550 aa)
secEPreprotein translocase subunit SecE; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation; Belongs to the SecE/SEC61-gamma family. (126 aa)
AOK51324.1General secretion pathway protein GspJ; Derived by automated computational analysis using gene prediction method: Protein Homology. (232 aa)
secYPreprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. (449 aa)
tatAPreprotein translocase subunit SecA; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. (77 aa)
tatBPreprotein translocase; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation. (175 aa)
Your Current Organism:
Burkholderia stagnalis
NCBI taxonomy Id: 1503054
Other names: B. stagnalis, Burkholderia sp. Bp6893, Burkholderia sp. Bp6916, Burkholderia sp. Bp7118, Burkholderia sp. Bp7119, Burkholderia sp. Bp7120, Burkholderia sp. Bp7137, Burkholderia sp. Bp7139, Burkholderia sp. Bp7142, Burkholderia sp. Bp7143, Burkholderia sp. Bp7145, Burkholderia sp. Bp7260, Burkholderia sp. Bp7266, Burkholderia sp. Bp7278, Burkholderia sp. Bp7280, Burkholderia sp. Bp7282, Burkholderia sp. Bp7288, Burkholderia sp. Bp7466, Burkholderia sp. Bp7469, Burkholderia sp. Bp7471, Burkholderia sp. Bp7483, Burkholderia sp. Bp7485, Burkholderia sp. Bp7491, Burkholderia sp. Bp7519, Burkholderia sp. Bp7520, Burkholderia sp. Bp7521, Burkholderia sp. Bp7554, Burkholderia sp. Bp7555, Burkholderia sp. Bp7571, Burkholderia sp. Bp7572, Burkholderia sp. Bp7635, Burkholderia sp. Bp7636, Burkholderia sp. Bp7639, Burkholderia sp. Bp7640, Burkholderia sp. Bp7641, Burkholderia sp. Bp7642, Burkholderia sp. Bp7643, Burkholderia sp. Bp7644, Burkholderia sp. Bp7645, Burkholderia sp. Bp7651, Burkholderia sp. Bp7656, Burkholderia sp. Bp7657, Burkholderia sp. Bp7658, Burkholderia sp. Bp7663, Burkholderia sp. Bp7665, Burkholderia sp. Bp7666, Burkholderia sp. Bp7667, Burkholderia sp. Bp7670, Burkholderia sp. Bp7671, Burkholderia sp. Bp7673, Burkholderia sp. Bp7681, Burkholderia sp. Bp7682, Burkholderia sp. Bp7684, Burkholderia sp. Bp7685, Burkholderia sp. Bp7686, Burkholderia sp. Bp7687, Burkholderia sp. Bp7690, Burkholderia sp. Bp7692, Burkholderia sp. Bp7693, Burkholderia sp. Bp7694, Burkholderia sp. Bp7697, Burkholderia sp. Bp7698, Burkholderia sp. Bp7699, Burkholderia sp. Bp7705, Burkholderia sp. Bp7707, Burkholderia sp. LMG 28156, Burkholderia sp. LMG 28157, Burkholderia sp. R-52095, Burkholderia sp. R-52096, Burkholderia sp. R-52235, Burkholderia sp. R-52237, Burkholderia sp. R-52238, Burkholderia sp. R-52240, Burkholderia stagnalis De Smet et al. 2015, CCUG 65686, LMG 28156, LMG:28156
Server load: low (24%) [HD]