STRINGSTRING
KQS48293.1 KQS48293.1 KQS48294.1 KQS48294.1 KQS48295.1 KQS48295.1 KQS48532.1 KQS48532.1 fliQ fliQ fliP fliP KQS48297.1 KQS48297.1 KQS48298.1 KQS48298.1 KQS48299.1 KQS48299.1 KQS48300.1 KQS48300.1 KQS48301.1 KQS48301.1 fliI fliI KQS48304.1 KQS48304.1 KQS48305.1 KQS48305.1 KQS48306.1 KQS48306.1 fliE fliE KQS48309.1 KQS48309.1 flhA-2 flhA-2 flgB flgB KQS48323.1 KQS48323.1 KQS48324.1 KQS48324.1 KQS48325.1 KQS48325.1 KQS48326.1 KQS48326.1 flgG flgG flgH flgH flgI-2 flgI-2 KQS48537.1 KQS48537.1 flgK flgK KQS48331.1 KQS48331.1 fliP-2 fliP-2 ASG20_16915 ASG20_16915 KQS46931.1 KQS46931.1 fliE-2 fliE-2 fliQ-2 fliQ-2 KQS46934.1 KQS46934.1 flhB flhB flgI flgI ASG20_16985 ASG20_16985 flhA flhA KQS47143.1 KQS47143.1 KQS47144.1 KQS47144.1 KQS46947.1 KQS46947.1 KQS46948.1 KQS46948.1 KQS46950.1 KQS46950.1 KQS47145.1 KQS47145.1 KQS47147.1 KQS47147.1 flgH-2 flgH-2 flgG-2 flgG-2 KQS46964.1 KQS46964.1 KQS46965.1 KQS46965.1
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:
KQS48293.1Flagellar export chaperone FliS; Derived by automated computational analysis using gene prediction method: Protein Homology. (132 aa)
KQS48294.1Hypothetical protein; Required for morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. (482 aa)
KQS48295.1Flagellar biosynthesis protein FlhB; Derived by automated computational analysis using gene prediction method: Protein Homology. (384 aa)
KQS48532.1Flagellar biosynthetic protein FliR; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (239 aa)
fliQFlagellar biosynthetic protein FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. (89 aa)
fliPFlagellar biosynthesis protein flip; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (262 aa)
KQS48297.1Flagellar biogenesis protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (84 aa)
KQS48298.1Flagellar 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. (96 aa)
KQS48299.1Flagellar motor switch protein FliM; Derived by automated computational analysis using gene prediction method: Protein Homology. (320 aa)
KQS48300.1Flagellar basal body protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (208 aa)
KQS48301.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (605 aa)
fliIFlagellar protein export ATPase FliI; Involved in type III protein export during flagellum assembly; Derived by automated computational analysis using gene prediction method: Protein Homology. (441 aa)
KQS48304.1Flagellar biosynthesis protein FliH; Derived by automated computational analysis using gene prediction method: Protein Homology. (253 aa)
KQS48305.1Flagellar motor switch protein FliG; Derived by automated computational analysis using gene prediction method: Protein Homology. (336 aa)
KQS48306.1Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. (557 aa)
fliEFlagellar hook-basal body protein FliE; Derived by automated computational analysis using gene prediction method: Protein Homology. (120 aa)
KQS48309.1Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (273 aa)
flhA-2Flagellar biosynthesis protein FlhA; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family. (686 aa)
flgBFlagellar biosynthesis protein FlgB; With FlgF and C makes up the proximal portion of the flagellar basal body rod; Vibrio parahaemolyticus protein is associated with the lateral flagella; Derived by automated computational analysis using gene prediction method: Protein Homology. (92 aa)
KQS48323.1Flagellar basal-body rod protein FlgC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the flagella basal body rod proteins family. (131 aa)
KQS48324.1Flagellar hook capping protein; Required for flagellar hook formation. May act as a scaffolding protein. (227 aa)
KQS48325.1Flagellar hook-basal body protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (426 aa)
KQS48326.1Flagellar biosynthesis protein FlgF; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the flagella basal body rod proteins family. (250 aa)
flgGFlagellar basal-body rod protein FlgG; Makes up the distal portion of the flagellar basal body rod; Bradyrhizobium has one thick flagellum and several thin flagella; the Bradyrhizobium protein in this cluster is associated with the thick flagella; Derived by automated computational analysis using gene prediction method: Protein Homology. (262 aa)
flgHFlagellar biosynthesis protein FlgH; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (231 aa)
flgI-2Flagellar biosynthesis protein FlgI; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (363 aa)
KQS48537.1Rod-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (108 aa)
flgKFlagellar biosynthesis protein FlgK; Derived by automated computational analysis using gene prediction method: Protein Homology. (448 aa)
KQS48331.1Hypothetical protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (306 aa)
fliP-2Flagellar biosynthetic protein flip; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (245 aa)
ASG20_16915Flagellar motor switch protein FliN; Derived by automated computational analysis using gene prediction method: Protein Homology. (78 aa)
KQS46931.1Flagellar basal-body rod protein FlgC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the flagella basal body rod proteins family. (135 aa)
fliE-2Flagellar hook-basal body protein FliE; Derived by automated computational analysis using gene prediction method: Protein Homology. (109 aa)
fliQ-2Flagellar biosynthetic protein FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. (87 aa)
KQS46934.1Flagellar biosynthetic protein FliR; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (254 aa)
flhBFlagellar biosynthetic protein FlhB; Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the type III secretion exporter family. (353 aa)
flgIFlagellar biosynthesis protein FlgA; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (369 aa)
ASG20_16985Basal-body rod modification protein FlgD; Required for flagellar hook formation. May act as a scaffolding protein. (221 aa)
flhAFlagellar biosynthesis protein FlhA; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family. (693 aa)
KQS47143.1Hypothetical protein; 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. (105 aa)
KQS47144.1Flagellar MS-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. (530 aa)
KQS46947.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (222 aa)
KQS46948.1Flagellar 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. (340 aa)
KQS46950.1Flagellar biosynthesis protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (143 aa)
KQS47145.1Flagellar protein export ATPase FliI; Derived by automated computational analysis using gene prediction method: Protein Homology. (457 aa)
KQS47147.1Flagellar biosynthesis protein FlgE; Derived by automated computational analysis using gene prediction method: Protein Homology. (414 aa)
flgH-2Flagellar biosynthesis protein FlgH; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (255 aa)
flgG-2Flagellar basal-body rod protein FlgG; Makes up the distal portion of the flagellar basal body rod; Bradyrhizobium has one thick flagellum and several thin flagella; the Bradyrhizobium protein in this cluster is associated with the thick flagella; Derived by automated computational analysis using gene prediction method: Protein Homology. (262 aa)
KQS46964.1Flagellar biosynthesis protein FlgF; Derived by automated computational analysis using gene prediction method: Protein Homology. (247 aa)
KQS46965.1Flagellar 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. (340 aa)
Your Current Organism:
Sphingomonas sp. Leaf198
NCBI taxonomy Id: 1736299
Other names: S. sp. Leaf198
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