STRINGSTRING
ANS87870.1 ANS87870.1 surA surA bamE bamE bamC bamC lptE lptE bamA bamA bamD bamD lptD lptD ANS86828.1 ANS86828.1 ANS86730.1 ANS86730.1 bamB bamB lptA lptA lptC lptC
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:
ANS87870.1Hypothetical protein. (150 aa)
surAPeptidylprolyl isomerase; 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. (431 aa)
bamEOuter membrane protein assembly factor BamE; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (127 aa)
bamCOuter membrane protein assembly factor BamC; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (340 aa)
lptELPS-assembly lipoprotein LptE; Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane. (220 aa)
bamAOuter membrane protein assembly factor BamA; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (800 aa)
bamDOuter membrane protein assembly factor BamD; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (241 aa)
lptDLPS-assembly protein LptD; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. (790 aa)
ANS86828.1Hypothetical protein. (380 aa)
ANS86730.1Hypothetical protein. (294 aa)
bamBOuter membrane protein assembly factor BamB; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (386 aa)
lptALipopolysaccharide export system protein LptA; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. May form a bridge between the inner membrane and the outer membrane, via interactions with LptC and LptD, thereby facilitating LPS transfer across the periplasm. (165 aa)
lptCHypothetical protein; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. Belongs to the LptC family. (187 aa)
Your Current Organism:
Vibrio scophthalmi
NCBI taxonomy Id: 45658
Other names: CAIM 75, CECT 4638, CIP 105211, LMG 19158, LMG:19158, V. scophthalmi, strain A089
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