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pagP pagP pal pal ompF ompF pqiA pqiA pqiB pqiB pqiC pqiC yebT yebT mlaA mlaA ftsH ftsH mlaB mlaB mlaC mlaC mlaD mlaD mlaE mlaE mlaF mlaF pldA pldA
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
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:
pagPPhospholipid:lipid A palmitoyltransferase; Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors. Phosphatidylglycerol (PtdGro), phosphatidylethanolamine (PtdEtn), phosphatidylserine (PtdSer) and phosphatidic acid (Ptd-OH) are all effective acyl donors. (186 aa)
palPeptidoglycan-associated outer membrane lipoprotein; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. The Tol-Pal system is also required for polar localization of chemoreceptors clusters. (173 aa)
ompFOuter membrane porin 1a (Ia;b;F); Forms pores that allow passive diffusion of small molecules across the outer membrane. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity; Belongs to the Gram-negative porin family. (362 aa)
pqiAParaquat-inducible, SoxRS-regulated inner membrane protein; Component of a transport pathway that contributes to membrane integrity; Belongs to the PqiA family. (417 aa)
pqiBParaquat-inducible, SoxRS-regulated MCE domain protein; Component of a transport pathway that contributes to membrane integrity. May directly span the intermembrane space, facilitating the transport of substrates across the periplasm (Probable); Belongs to the PqiB family. (546 aa)
pqiCDUF330 family putative lipoprotein; Component of a transport pathway that contributes to membrane integrity. (187 aa)
yebTMCE domain protein; Component of a transport pathway that contributes to membrane integrity. May directly span the intermembrane space, facilitating the transport of substrates across the periplasm (Probable); Belongs to the PqiB family. (877 aa)
mlaAABC transporter maintaining OM lipid asymmetry, OM lipoprotein component; Involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Belongs to the MlaA family. (251 aa)
ftsHProtease, ATP-dependent zinc-metallo; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent [...] (644 aa)
mlaBABC transporter maintaining OM lipid asymmetry, cytoplasmic STAS component; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaB plays critical roles in both the assembly and activity of the complex. May act by modulating MlaF structure and stability. (97 aa)
mlaCABC transporter maintaining OM lipid asymmetry, periplasmic binding protein; Involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. May transfer phospholipid across the periplasmic space and deliver it to the MlaFEDB complex at the inner membrane. Belongs to the MlaC/ttg2D family. (211 aa)
mlaDOM lipid asymmetry maintenance protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaD functions in substrate binding with strong affinity for phospholipids and modulates ATP hydrolytic activity of the complex. (183 aa)
mlaEABC transporter maintaining OM lipid asymmetry, inner membrane permease protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Probably responsible for the translocation of the substrate across the membrane. Belongs to the MlaE permease family. (260 aa)
mlaFABC transporter maintaining OM lipid asymmetry, ATP-binding protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Responsible for energy coupling to the transport system. (269 aa)
pldAOuter membrane phospholipase A; Has broad substrate specificity including hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. Strong expression leads to outer membrane breakdown and cell death; is dormant in normal growing cells. Required for efficient secretion of bacteriocins. (289 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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