STRINGSTRING
secE secE tatC2 tatC2 tatC1 tatC1 ftsY ftsY secY secY secD secD secF secF tatA1 tatA1 tatA2 tatA2 srp19 srp19 srp54 srp54 Nmlp_3404 Nmlp_3404 sec11 sec11
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:
secEProtein 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. (57 aa)
tatC2Sec-independent protein translocase 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. (777 aa)
tatC1Sec-independent protein translocase 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. (259 aa)
ftsYSignal recognition particle receptor 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). (359 aa)
secYProtein 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. (492 aa)
secDProtein-export membrane protein SecD; Involved in protein export. (532 aa)
secFProtein-export membrane protein SecF; Involved in protein export. (283 aa)
tatA1Sec-independent protein translocase subunit TatA; 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. (140 aa)
tatA2Sec-independent protein translocase subunit TatA; 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. (92 aa)
srp19Signal recognition particle 19K protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP. (92 aa)
srp54Signal recognition particle 54K protein; 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. Belongs to the GTP-binding SRP family. SRP54 subfamily. (464 aa)
Nmlp_3404Peptidase S26 domain protein. (384 aa)
sec11Signal peptidase I. (294 aa)
Your Current Organism:
Natronomonas moolapensis
NCBI taxonomy Id: 268739
Other names: N. moolapensis 8.8.11, Natronomonas moolapensis 8.8.11, Natronomonas moolapensis DSM 18674, Natronomonas moolapensis JCM 14361, Natronomonas moolapensis str. 8.8.11, Natronomonas moolapensis strain 8.8.11, haloarchaeon CSW8.8.11
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