STRINGSTRING
lolB lolB lptE lptE bamE bamE bamB bamB ARD39245.1 ARD39245.1 ARD39248.1 ARD39248.1 ARD39249.1 ARD39249.1 bamD bamD ARD39949.1 ARD39949.1 ARD39950.1 ARD39950.1 lptD lptD djlA djlA bamC bamC
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:
lolBOuter membrane lipoprotein LolB; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. (206 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. (224 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. (116 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. (392 aa)
ARD39245.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (206 aa)
ARD39248.1Helix-turn-helix domain-containing protein; Cytoskeletal protein that is involved in cell-shape control through regulation of the length of the long axis. Belongs to the RodZ family. (341 aa)
ARD39249.1Type IV pilus biogenesis/stability protein PilW; Derived by automated computational analysis using gene prediction method: Protein Homology. (250 aa)
bamDHypothetical protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamA, the core component of the assembly machinery. (245 aa)
ARD39949.1Protoheme IX biogenesis protein HemY; Derived by automated computational analysis using gene prediction method: Protein Homology. (399 aa)
ARD39950.1uroporphyrinogen-III C-methyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. (382 aa)
lptDLPS assembly protein LptD; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. (795 aa)
djlAMolecular chaperone DjlA; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host. (273 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. (346 aa)
Your Current Organism:
Edwardsiella ictaluri
NCBI taxonomy Id: 67780
Other names: ATCC 33202, CCUG 18764, CIP 81.96, DSM 13697, E. ictaluri, JCM 16934, NCTC 12122, SECFDL GA 77-52
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