STRINGSTRING
secE secE secY secY tatA tatA tatB tatB tatC tatC secA secA ffh ffh secF secF secD secD yajC yajC AOK52251.1 AOK52251.1 AOK53329.1 AOK53329.1 lspA lspA ftsY ftsY secB secB yidC yidC
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:
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)
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)
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)
ffhSignal recognition particle; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components; Belo [...] (455 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)
yajCPreprotein translocase subunit YajC; The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-YajC-YidC subcomplex facilitates these functions. (108 aa)
AOK52251.1S26 family signal peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase S26 family. (297 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)
lspASignal peptidase II; This protein specifically catalyzes the removal of signal peptides from prolipoproteins; Belongs to the peptidase A8 family. (166 aa)
ftsYSignal recognition particle-docking protein FtsY; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components. (389 aa)
secBPreprotein translocase subunit SecB; One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA. (160 aa)
yidCInsertase; Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins. (556 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
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