STRINGSTRING
lpg2962 lpg2962 lpg0657 lpg0657 lpg0896 lpg0896 lpg0906 lpg0906 lpg0907 lpg0907 lpg0908 lpg0908 flgB flgB flgC flgC flgD flgD flgE flgE flgF flgF flgG flgG flgH flgH flgI flgI flgK flgK flgL flgL fliS fliS fliD fliD fliC fliC lpg1496 lpg1496 lpg1688 lpg1688 fliJ fliJ fliI fliI fliH fliH fliG fliG fliF fliF fliE fliE motB motB motA motA fliA fliA flhA flhA flhB flhB fliR fliR fliQ fliQ fliP fliP fliO fliO lpg1791 lpg1791 fliM fliM pal pal legA6 legA6 motA-2 motA-2 motB-2 motB-2 lpg2582 lpg2582
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:
lpg2962Sodium-type flagellar protein. (299 aa)
lpg0657Outer membrane protein, OmpA family protein. (249 aa)
lpg0896Hypothetical protein. (125 aa)
lpg0906Flagellar biosynthesis/type III secretory pathway chaperone. (165 aa)
lpg0907Negative regulator of flagellin synthesis. (106 aa)
lpg0908Flagella basal body P-ring formation protein FlgA; 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. (233 aa)
flgBFlagellar basal body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (130 aa)
flgCFlagellar basal body rod protein FlgC. (140 aa)
flgDFlagellar basal body rod modification protein FlgD; Required for flagellar hook formation. May act as a scaffolding protein. (225 aa)
flgEFlagellar hook protein FlgE. (437 aa)
flgFFlagellar basal body rod protein FlgF; Belongs to the flagella basal body rod proteins family. (248 aa)
flgGFlagellar basal body rod protein FlgG; Belongs to the flagella basal body rod proteins family. (261 aa)
flgHFlagellar 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. (230 aa)
flgIFlagellar P-ring protein (precursor) FlgI; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (394 aa)
flgKFlagellar hook associated protein 1 FlgK; Belongs to the flagella basal body rod proteins family. (649 aa)
flgLFlagellar hook associated protein type 3 FlgL. (411 aa)
fliSFlagellar protein FliS. (136 aa)
fliDFlagellar hook associated protein 2 FliD; 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. (541 aa)
fliCFlagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (475 aa)
lpg1496Hypothetical protein. (598 aa)
lpg1688Possible flagellar hook-length control protein. (414 aa)
fliJFlagellar protein FliJ. (151 aa)
fliINucleotide binding protein FliI. (450 aa)
fliHFlagellar assembly protein FliH. (212 aa)
fliGFlagellar 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. (329 aa)
fliFFlagellar basal body M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. (544 aa)
fliEFlagellar hook-basal body protein FliE. (104 aa)
motBFlagellar motor protein MotB. (273 aa)
motAFlagellar motor protein MotA. (257 aa)
fliAFlagellar biosynthesis sigma factor FliA; 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. (262 aa)
flhAFlagellar biosynthetic 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. (692 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. (383 aa)
fliRFlagellar biosynthetic protein FliR; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (256 aa)
fliQFlagellar biosynthetic protein FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. (89 aa)
fliPFlagellar biosynthetic protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (249 aa)
fliOFlagellar assembly protein FliO. (136 aa)
lpg1791Flagellar 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. (109 aa)
fliMFlagellar protein; 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. (355 aa)
palPeptidoglycan associated lipoprotein; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. (176 aa)
legA6Ankyrin 3; Conserved gene; node of Ranvier. (180 aa)
motA-2Chemotaxis (motility protein A) transmembrane. (301 aa)
motB-2Chemotaxis (motility protein B) transmembrane. (312 aa)
lpg2582Hypothetical protein. (388 aa)
Your Current Organism:
Legionella pneumophila Philadelphia
NCBI taxonomy Id: 272624
Other names: L. pneumophila subsp. pneumophila str. Philadelphia 1, Legionella pneumophila subsp. pneumophila str. Philadelphia 1, Legionella pneumophila subsp. pneumophila str. Philadelphia-1, Legionella pneumophila subsp. pneumophila strain Philadelphia 1
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