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fhiA fhiA lfhB lfhB lfiR lfiR lfiQ lfiQ lfiP lfiP lfiN lfiN lfiM lfiM lfiE lfiE lfiF lfiF lfiG lfiG lfiH lfiH lgiI lgiI lfgA lfgA lfgB lfgB lfgC lfgC lfdD lfdD lfgE lfgE lfgF lfgF lfgG lfgG lfgH lfgH lfgI lfgI lfgJ lfgJ lfgK lfgK lfgL lfgL lafA lafA lafB lafB lafC lafC lafE lafE lafF lafF CAR11506.1 CAR11506.1 lafT lafT mbhA mbhA flgB flgB flgC flgC flgD flgD flgE flgE flgF flgF flgG flgG flgH flgH flgI flgI flgJ flgJ flgK flgK flgL flgL flhA flhA flhB flhB motB motB motA motA CAR13408.1 CAR13408.1 fliE fliE fliF fliF fliG fliG fliH fliH fliI fliI fliJ fliJ fliK fliK fliL fliL fliM fliM fliN fliN fliO fliO fliP fliP fliQ fliQ fliR fliR
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:
fhiAFlagellar system 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. (697 aa)
lfhBLateral flagellar export/assembly protein (FlhB-like); Function of strongly homologous gene; transporter. (379 aa)
lfiRFlagellar biosynthetic protein fliR; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (260 aa)
lfiQLateral flagellar export/assembly protein (FliQ-like); Function of strongly homologous gene; structure. (90 aa)
lfiPLateral flagellar export/assembly protein, FliP-like; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (250 aa)
lfiNLateral flagellar export/assembly protein, Flagellar motor switch (C ring) (FliN-like); Function of strongly homologous gene; cell process. (123 aa)
lfiMLateral flagellar export/assembly protein Flagellar motor switch C-ring (FliM-like); Function of strongly homologous gene; cell process. (283 aa)
lfiELateral flagellar basal body component protein (FliE-like); Function of strongly homologous gene; structure. (113 aa)
lfiFLateral flagellar M-ring protein (FliF-like); The M ring may be actively involved in energy transduction. Belongs to the FliF family. (548 aa)
lfiGLateral flagellar C-ring switch protein (LfiG-like); Function of strongly homologous gene; cell process. (336 aa)
lfiHLateral flagellar export/assembly protein (LfiH-like); Function of strongly homologous gene; structure. (236 aa)
lgiIFlagellum-specific ATP synthase, Lateral flagellar export/assembly protein; Function of strongly homologous gene; enzyme. (445 aa)
lfgALateral flagellar P-ring addition protein (FlgA-like); 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. (245 aa)
lfgBLateral flagellar rod protein (FlgB-like); Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (121 aa)
lfgCPutative Flagellar basal-body rod protein flgC (proximal rod protein); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative structure; Belongs to the flagella basal body rod proteins family. (143 aa)
lfdDLateral flagellar rod protein (FlgD-like); Required for flagellar hook formation. May act as a scaffolding protein. (237 aa)
lfgELateral flagellar hook protein (FlgE-like); Function of strongly homologous gene; structure. (400 aa)
lfgFLateral flagellar rod protein (FlgF-like); Function of strongly homologous gene; structure. (245 aa)
lfgGFlagellar basal-body rod protein (flgG-like) (Distal rod protein); Function of strongly homologous gene; structure; Belongs to the flagella basal body rod proteins family. (303 aa)
lfgHFlagellar L-ring protein 2 precursor (Basal body L-ring protein 2) (FlgH-like); Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (221 aa)
lfgIFlagellar P-ring protein 2 precursor (Basal body P-ring protein 2)(flgL-like); Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (371 aa)
lfgJLateral flagellar peptidoglycan hydrolase (FlgJ-like); Function of strongly homologous gene; enzyme. (99 aa)
lfgKLateral flagellar hook associated protein 1 (FlgK-like); Function of strongly homologous gene; structure. (458 aa)
lfgLLateral flagellar hook associated protein 3 (FlgL-like); Function of strongly homologous gene; structure. (309 aa)
lafALateral flagellin (FliC-like); Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (326 aa)
lafBLateral flagellar hook associated protein 2 (FliD-like); 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. (438 aa)
lafCLateral flagellar chaperone protein (FliS-like); Function of strongly homologous gene; factor. (130 aa)
lafELateral flagellar hook length control protein (FliK-like); Function of strongly homologous gene; structure. (352 aa)
lafFLateral flagellar associated protein (FliL-like); Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (155 aa)
CAR11506.1Putative RNA polymerase sigma factor for flagellar operon (FliA/lafS-like); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator; Belongs to the sigma-70 factor family. (238 aa)
lafTChemotaxis protein lafT, Lateral flagellar motor protein A (MotA-like); Function of strongly homologous gene; structure. (287 aa)
mbhAFlagellar system protein; Function of strongly homologous gene; structure. (307 aa)
flgBFlagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (138 aa)
flgCFlagellar component of cell-proximal portion of basal-body rod; Function experimentally demonstrated in the studied species; structure; Belongs to the flagella basal body rod proteins family. (134 aa)
flgDFlagellar hook assembly protein; Required for flagellar hook formation. May act as a scaffolding protein. (231 aa)
flgEFlagellar hook protein; Function experimentally demonstrated in the studied species; structure. (401 aa)
flgFFlagellar component of cell-proximal portion of basal-body rod; Function experimentally demonstrated in the studied species; structure. (251 aa)
flgGFlagellar component of cell-distal portion of basal-body rod; Function experimentally demonstrated in the studied species; structure; Belongs to the flagella basal body rod proteins family. (260 aa)
flgHFlagellar protein of basal-body outer-membrane L ring; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (232 aa)
flgIFlagellar basal body 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)
flgJMuramidase; Function experimentally demonstrated in the studied species; enzyme. (313 aa)
flgKFlagellar hook-filament junction protein 1; Function experimentally demonstrated in the studied species; structure. (547 aa)
flgLFlagellar hook-filament junction protein; Function experimentally demonstrated in the studied species; structure. (317 aa)
flhAPutative flagellar export pore 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. (692 aa)
flhBFlagellar export pore protein; 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. (382 aa)
motBProtein that enables flagellar motor rotation; Function experimentally demonstrated in the studied species; cell process. (308 aa)
motAProton conductor component of flagella motor; Function experimentally demonstrated in the studied species; cell process. (295 aa)
CAR13408.1FliC Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (554 aa)
fliEFlagellar basal-body component; Function experimentally demonstrated in the studied species; structure. (104 aa)
fliFFlagellar basal-body MS-ring and collar protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. (552 aa)
fliGFlagellar motor switching and energizing component; 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. (331 aa)
fliHFlagellar biosynthesis protein; Function experimentally demonstrated in the studied species; structure. (228 aa)
fliIFlagellum-specific ATP synthase; Function experimentally demonstrated in the studied species; enzyme. (457 aa)
fliJFlagellar protein; Flagellar protein that affects chemotactic events. Belongs to the FliJ family. (147 aa)
fliKFlagellar hook-length control protein; Function experimentally demonstrated in the studied species; structure. (375 aa)
fliLFlagellar biosynthesis protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (154 aa)
fliMFlagellar motor switching and energizing component; 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. (334 aa)
fliNFlagellar motor switching and energizing component; 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)
fliOFlagellar biosynthesis protein; Function experimentally demonstrated in the studied species; structure. (121 aa)
fliPFlagellar biosynthesis protein; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (245 aa)
fliQFlagellar biosynthesis protein; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. (89 aa)
fliRFlagellar export pore protein; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (261 aa)
Your Current Organism:
Escherichia coli UMN026
NCBI taxonomy Id: 585056
Other names: E. coli UMN026
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