STRINGSTRING
fliC fliC dnaK dnaK fepE fepE fljB fljB prgJ prgJ prgI prgI sipA sipA sipD sipD sipC sipC invA invA
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:
fliCFlagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (495 aa)
dnaKChaperone Hsp70; Acts as a chaperone. (638 aa)
fepESimilar to E. coli ferric enterobactin (enterochelin) transport (AAC73688.1); Blastp hit to AAC73688.1 (377 aa), 73% identity in aa 1 - 373. (378 aa)
fljBFilament structural protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (506 aa)
prgJCytoplasmic cell invasion protein; Required for invasion of epithelial cells. (101 aa)
prgICytoplasmic cell invasion protein; Required for invasion of epithelial cells; Belongs to the MxiH/PrgI/YscF family. (80 aa)
sipACell invasion protein; Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F- actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments; [...] (685 aa)
sipDCell invasion protein; Required for translocation of effector proteins via the type III secretion system SPI-1, which is essential for an efficient bacterial internalization. Probably acts by modulating the secretion of SipA, SipB, and SipC. (343 aa)
sipCCell invasion protein; Actin-binding protein that interferes with host cell actin cytoskeleton. Nucleates actin polymerization and condensates actin filaments into cables (bundling). SipA potenciates SipC activity and both are required for an efficient bacterial internalization by the host cell. (409 aa)
invAInvasion protein; Involved in the invasion of the cells of the intestinal epithelium. Could be involved in the translocation of the InvE protein; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family. (685 aa)
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.