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flhC flhC frdC frdC lfgN lfgN flgM flgM flgA flgA flgD flgD flgJ flgJ flgK flgK fliR fliR fliQ fliQ fliP fliP fliO fliO fliK fliK fliJ fliJ fliI fliI fliS fliS AZKH_1516 AZKH_1516 flhD flhD AZKH_3362 AZKH_3362 AZKH_3464 AZKH_3464 flhF flhF flhA flhA fliW fliW
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:
flhCTranscriptional activator; Functions in complex with FlhD as a master transcriptional regulator that regulates transcription of several flagellar and non- flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways; Belongs to the FlhC family. (183 aa)
frdCFumarate reductase, subunit C. (135 aa)
lfgNPutative chaperon of flagellar synthesis. (157 aa)
flgMPutative negative regulator of flagellin synthesis. (98 aa)
flgAChaperon for flagellar basal body P-ring formation; Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P- ring assembly; Belongs to the FlgA family. (236 aa)
flgDBasal-body rod modification protein; Required for flagellar hook formation. May act as a scaffolding protein. (225 aa)
flgJPeptidoglycan hydrolase. (346 aa)
flgKFlagellar hook-filament junction protein 1. (482 aa)
fliRFlagellar biosynthesis protein; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (266 aa)
fliQFlagellar biosynthesis protein; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. (89 aa)
fliPFlagellar biosynthesis protein; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (253 aa)
fliOFlagellar biosynthesis protein. (140 aa)
fliKFlagellar hook-length control protein. (510 aa)
fliJFlagellar protein. (151 aa)
fliIFlagellar-specific ATP synthase. (467 aa)
fliSFlagellar protein. (137 aa)
AZKH_1516Hypothetical protein. (1919 aa)
flhDFlagellar transcriptional activator; Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non- flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways; Belongs to the FlhD family. (106 aa)
AZKH_3362Hypothetical protein. (257 aa)
AZKH_3464Hypothetical protein. (151 aa)
flhFFlagellar biosynthesis regulator. (516 aa)
flhAFlagellar biosynthesis protein; 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. (702 aa)
fliWFlagellar assembly protein; Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum. (147 aa)
Your Current Organism:
Azoarcus sp. KH32C
NCBI taxonomy Id: 748247
Other names: A. sp. KH32C
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