STRINGSTRING
Spea_2816 Spea_2816 torD torD secY secY Spea_3864 Spea_3864 Spea_4139 Spea_4139 napD-2 napD-2 surA surA napD napD
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.
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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
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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:
Spea_2816PFAM: cytoplasmic chaperone TorD family protein; KEGG: sfr:Sfri_3126 cytoplasmic chaperone TorD family protein. (241 aa)
torDCytoplasmic chaperone TorD family protein; Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor; Belongs to the TorD/DmsD family. TorD subfamily. (221 aa)
secYPreprotein translocase, SecY subunit; 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. (446 aa)
Spea_3864PFAM: cytoplasmic chaperone TorD family protein; KEGG: sfr:Sfri_3126 cytoplasmic chaperone TorD family protein. (206 aa)
Spea_4139PFAM: cytoplasmic chaperone TorD family protein; KEGG: slo:Shew_0057 cytoplasmic chaperone TorD family protein. (224 aa)
napD-2NapD family protein; Chaperone for NapA, the catalytic subunit of the periplasmic nitrate reductase. It binds directly and specifically to the twin- arginine signal peptide of NapA, preventing premature interaction with the Tat translocase and premature export. (85 aa)
surASurA domain; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. (434 aa)
napDNapD family protein; Chaperone for NapA, the catalytic subunit of the periplasmic nitrate reductase. It binds directly and specifically to the twin- arginine signal peptide of NapA, preventing premature interaction with the Tat translocase and premature export. (91 aa)
Your Current Organism:
Shewanella pealeana
NCBI taxonomy Id: 398579
Other names: S. pealeana ATCC 700345, Shewanella pealeana ATCC 700345, Shewanella pealeana str. ATCC 700345, Shewanella pealeana strain ATCC 700345
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