STRINGSTRING
CCO56762.1 CCO56762.1 CCO56763.1 CCO56763.1 CCO56764.1 CCO56764.1 pomA pomA motB motB flaD-4 flaD-4 fliDP fliDP flaJ flaJ fliE fliE CCO56898.1 CCO56898.1 fliG fliG CCO56900.1 CCO56900.1 fliI fliI CCO56902.1 CCO56902.1 CCO56903.1 CCO56903.1 CCO56904.1 CCO56904.1 fliM fliM fliN fliN CCO56907.1 CCO56907.1 fliP fliP fliQ fliQ CCO56910.1 CCO56910.1 flhB flhB flhA flhA CCO56913.1 CCO56913.1 fleN fleN fliA fliA flgL flgL flgM flgM flgJ flgJ flgI flgI flgH flgH flgG flgG flgF flgF flgE flgE CCO58693.1 CCO58693.1 CCO58694.1 CCO58694.1 CCO58695.1 CCO58695.1 CCO58699.1 CCO58699.1 CCO58700.1 CCO58700.1 CCO59697.1 CCO59697.1
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:
CCO56762.1Putative Flagellar motor rotation protein MotB; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component. (214 aa)
CCO56763.1Putative Flagellar motor rotation protein MotA; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component. (259 aa)
CCO56764.1Putative Flagellar motor switch protein FliG; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component. (601 aa)
pomAChemotaxis protein pomA; Function experimentally demonstrated in the studied genus; membrane component. (254 aa)
motBSodium-driven polar flagellar protein; Function experimentally demonstrated in the studied genus; membrane component. (313 aa)
flaD-4Flagellin D; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (376 aa)
fliDPPolar flagellar hook-associated protein 2; 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. (624 aa)
flaJFlagellar protein FlaJ; Function experimentally demonstrated in the studied genus; membrane component. (136 aa)
fliEFlagellar hook-basal body complex protein fliE; Function of homologous gene experimentally demonstrated in an other organism; membrane component. (103 aa)
CCO56898.1Putative Flagellar M-ring protein fliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. (578 aa)
fliGFlagellar motor switch protein G; 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. (350 aa)
CCO56900.1Putative flagellar assembly protein H; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component. (266 aa)
fliIFlagellum-specific ATP synthase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (451 aa)
CCO56902.1Putative Flagellar protein fliJ; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. (147 aa)
CCO56903.1Putative Flagellar hook-length control protein fliK; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component. (690 aa)
CCO56904.1Putative Flagellar biosynthesis protein fliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (164 aa)
fliMFlagellar 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. (359 aa)
fliNFlagellar 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. (135 aa)
CCO56907.1Putative Flagellar biosynthesis protein FliO; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component. (126 aa)
fliPFlagellar biosynthesis protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (289 aa)
fliQPutative flagellar biosynthesis protein FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. (89 aa)
CCO56910.1Putative Flagellar biosynthesis protein FliR; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (260 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. (376 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. (697 aa)
CCO56913.1Putative Flagellar biosynthesis protein FlhF; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (494 aa)
fleNFlagellar number regulator (Flagellar synthesis regulator FleN); Function of homologous gene experimentally demonstrated in an other organism; regulator. (295 aa)
fliARNA polymerase sigma factor for flagellar operon; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes; Belongs to the sigma-70 factor family. FliA subfamily. (244 aa)
flgLFlagellar Hook associated protein; Function experimentally demonstrated in the studied genus; structure. (397 aa)
flgMFlagellar hook-associated protein; Function experimentally demonstrated in the studied genus; structure. (626 aa)
flgJPeptidoglycan hydrolase flgJ; Function experimentally demonstrated in the studied genus; enzyme. (303 aa)
flgIFlagellar P-ring protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (365 aa)
flgHPutative Flagellar L-ring protein FlgH; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (258 aa)
flgGFlagellar basal-body rod protein flgG; Function of homologous gene experimentally demonstrated in an other organism; structure; Belongs to the flagella basal body rod proteins family. (262 aa)
flgFFlagellar basal body rod protein FlgF; Function experimentally demonstrated in the studied genus; structure. (249 aa)
flgEFlagellar hook protein FlgE; Function experimentally demonstrated in the studied genus; structure. (434 aa)
CCO58693.1Putative Flagellar basal-body rod modification protein FlgD; Required for flagellar hook formation. May act as a scaffolding protein. (235 aa)
CCO58694.1Putative Flagellar basal-body rod protein FlgC; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; structure; Belongs to the flagella basal body rod proteins family. (138 aa)
CCO58695.1Putative Flagellar basal-body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (131 aa)
CCO58699.1Putative Flagellar basal-body P-ring formation protein flgA; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure. (257 aa)
CCO58700.1Putative Negative regulator of flagellin synthesis FlgM (anti-sigma28 factor); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (103 aa)
CCO59697.1Putative Flagellar basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (136 aa)
Your Current Organism:
Vibrio nigripulchritudo
NCBI taxonomy Id: 28173
Other names: ATCC 27043, Beneckea nigrapulchrituda, Beneckea nigripulchritudo, CAIM 323, CCUG 28586, CIP 103195, LMG 3896, LMG:3896, V. nigripulchritudo
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