STRINGSTRING
ARD38109.1 ARD38109.1 motB motB ARD38111.1 ARD38111.1 ARD38112.1 ARD38112.1 ARD38113.1 ARD38113.1 ARD38114.1 ARD38114.1 ARD38115.1 ARD38115.1 cheB cheB ARD38117.1 ARD38117.1 ARD38118.1 ARD38118.1 ARD38476.1 ARD38476.1 ARD38703.1 ARD38703.1 ARD38709.1 ARD38709.1 ARD38710.1 ARD38710.1 ARD38825.1 ARD38825.1 ARD38988.1 ARD38988.1 ARD39298.1 ARD39298.1 ARD39723.1 ARD39723.1 ARD39737.1 ARD39737.1 ARD39831.1 ARD39831.1 ARD40034.1 ARD40034.1
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:
ARD38109.1Flagellar motor stator protein MotA; Derived by automated computational analysis using gene prediction method: Protein Homology. (301 aa)
motBFlagellar motor protein MotB; With MotA forms the ion channels that couple flagellar rotation to proton/sodium motive force across the membrane and forms the stator elements of the rotary flagellar machine; Derived by automated computational analysis using gene prediction method: Protein Homology. (334 aa)
ARD38111.1Chemotaxis protein CheA; Derived by automated computational analysis using gene prediction method: Protein Homology. (712 aa)
ARD38112.1Chemotaxis protein CheW; Derived by automated computational analysis using gene prediction method: Protein Homology. (164 aa)
ARD38113.1Methyl-accepting chemotaxis protein II; Serine sensor receptor; Derived by automated computational analysis using gene prediction method: Protein Homology. (555 aa)
ARD38114.1Methyl-accepting chemotaxis protein; Mediates taxis toward dipeptides; Derived by automated computational analysis using gene prediction method: Protein Homology. (532 aa)
ARD38115.1Chemotaxis protein-glutamate O-methyltransferase; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. (291 aa)
cheBChemotaxis response regulator protein-glutamate methylesterase; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Belongs to the CheB family. (350 aa)
ARD38117.1Chemotaxis regulator that, when phosphorylated, interacts with the flagellar motor causing the flagella to spin clockwise which causes the cell to tumble; Derived by automated computational analysis using gene prediction method: Protein Homology. (129 aa)
ARD38118.1Protein phosphatase CheZ; Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). (213 aa)
ARD38476.1Chemotaxis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (596 aa)
ARD38703.1Flagellar motor switch protein FliG; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. (330 aa)
ARD38709.1Flagellar motor switch protein FliM; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. (337 aa)
ARD38710.1Flagellar motor switch protein FliN; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family. (137 aa)
ARD38825.1Chemotaxis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (528 aa)
ARD38988.1Methyl-accepting chemotaxis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (554 aa)
ARD39298.1Chemotaxis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (526 aa)
ARD39723.1Methyl-accepting chemotaxis protein II; Serine sensor receptor; Derived by automated computational analysis using gene prediction method: Protein Homology. (525 aa)
ARD39737.1ABC transporter substrate-binding protein; DppABCDF is involved in the transport of dipeptides; also binds heme and mediates chemotaxis to dipeptides; Derived by automated computational analysis using gene prediction method: Protein Homology. (542 aa)
ARD39831.1D-ribose ABC transporter substrate-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (295 aa)
ARD40034.1Maltose ABC transporter substrate-binding protein MalE; Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Binds maltose and higher maltodextrins. Belongs to the bacterial solute-binding protein 1 family. (397 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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