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CHR53_24585 CHR53_24585 flhF flhF flhA flhA flhB flhB fliR fliR fliQ fliQ fliP fliP CHR53_24620 CHR53_24620 fliN fliN fliJ fliJ fliI fliI CHR53_24640 CHR53_24640 fliG fliG fliF fliF fliE fliE flgC flgC flgB flgB fliS fliS fliN-2 fliN-2 fliM fliM flgG flgG CHR53_24695 CHR53_24695 CHR53_24700 CHR53_24700 CHR53_24710 CHR53_24710 CHR53_24720 CHR53_24720 flgL flgL CHR53_24740 CHR53_24740 CHR53_24755 CHR53_24755 CHR53_24760 CHR53_24760 CHR53_24770 CHR53_24770 CHR53_24775 CHR53_24775
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:
CHR53_24585Unannotated protein. (290 aa)
flhFUnannotated protein. (387 aa)
flhAUnannotated 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. (676 aa)
flhBUnannotated 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. (364 aa)
fliRUnannotated protein; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (226 aa)
fliQUnannotated protein; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. (89 aa)
fliPUnannotated protein; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (249 aa)
CHR53_24620Unannotated protein. (200 aa)
fliNUnannotated 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. (115 aa)
fliJUnannotated protein. (148 aa)
fliIUnannotated protein. (441 aa)
CHR53_24640Unannotated protein. (262 aa)
fliGUnannotated protein; One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation; Belongs to the FliG family. (333 aa)
fliFUnannotated protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. (535 aa)
fliEUnannotated protein. (98 aa)
flgCUnannotated protein; Belongs to the flagella basal body rod proteins family. (146 aa)
flgBUnannotated protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (134 aa)
fliSUnannotated protein. (120 aa)
fliN-2Unannotated 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. (124 aa)
fliMUnannotated protein; One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation; Belongs to the FliM family. (313 aa)
flgGUnannotated protein. (273 aa)
CHR53_24695Unannotated protein. (138 aa)
CHR53_24700Unannotated protein. (361 aa)
CHR53_24710Unannotated 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. (520 aa)
CHR53_24720Unannotated protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (422 aa)
flgLUnannotated protein. (292 aa)
CHR53_24740Unannotated protein. (488 aa)
CHR53_24755Unannotated protein. (258 aa)
CHR53_24760Unannotated protein. (280 aa)
CHR53_24770Unannotated protein. (266 aa)
CHR53_24775Unannotated protein. (241 aa)
Your Current Organism:
Bacillus mesonae
NCBI taxonomy Id: 1193713
Other names: B. mesonae, Bacillus mesonae Liu et al. 2014, Bacillus sp. FJAT-13985, CGMCC1.12238, DSM 25968, strain FJAT-13985
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