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prgH prgH sipB sipB sicA sicA invA invA invF invF ydeW ydeW lexA lexA fliM fliM fliN fliN sopA sopA prgK prgK fliG fliG sdiA sdiA cheY cheY nmpC nmpC ompA ompA
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:
prgHCell invasion protein; Required for invasion of epithelial cells. (392 aa)
sipBCell invasion protein; Required for entry into the host cell through presentation or delivery of SipC at the host cell plasma membrane. Along with SipC, is necessary for the transfer of other effector proteins into the host cell. Induces macrophage apoptosis either by binding and activating the proapoptotic enzyme caspase-1 (caspase-1 dependent), resulting in the release of interleukin-1 beta active form, or by disrupting mitochondria and inducing autophagy (caspase-1 independent). The former is dependent of its membrane-fusion activity. The SipBC complex, in association with its chape [...] (593 aa)
sicASurface presentation of antigens; Type III secretion-associated chaperone required for SipB and SipC stabilization. Prevents premature association of SipB with SipC, which may lead to their targeting for degradation. Along with InvF, required for transcription activation of sigDE (sopB pipC), sicAsipBCDA, and sopE. (165 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)
invFInvasion protein; Transcriptional regulator required for the expression of several genes encoding type III secretion system SPI1 effector proteins. The interaction with SicA is necessary for the activation of sigDE (sopB pipC), sicAsipBCDA, and sopE. (216 aa)
ydeWPutative transcriptional repressor; In the absence of autoinducer 2 (AI-2), represses transcription of the lsrACDBFGE operon and its own transcription. In the presence of AI-2, LsrR is inactivated by binding phospho-AI-2, leading to the transcription of the lsr genes. (319 aa)
lexASOS response regulator; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single- stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. (202 aa)
fliMFlagellar biosynthesis 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 (By similarity). (334 aa)
fliNFlagellar biosynthesis 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 (By similarity). Belongs to the FliN/MopA/SpaO family. (137 aa)
sopASecreted effector protein of Salmonella; Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Required for inducing polymorphonuclear leukocytes migration across the intestinal epithelium. Preferentially uses host UBE2D1 (UBCH5A), UBE2D2 (UBCH5B) and UBE2L3 (UBCH7) as E2 ubiquitin-conjugating enzymes. (782 aa)
prgKCell invasion protein; Required for invasion of epithelial cells. Could be involved in protein secretion; Belongs to the YscJ lipoprotein family. (252 aa)
fliGFlagellar biosynthesis protein; 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 (By similarity). (331 aa)
sdiALuxR/UhpA family; similar to E. coli transcriptional regulator of ftsQAZ gene cluster (AAC74983.1); Blastp hit to AAC74983.1 (240 aa), 71% identity in aa 1 - 240. (240 aa)
cheYChemotaxis regulator protein; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Shows autophosphatase activity which is enhanced by CheZ. (129 aa)
nmpCNew outer membrane protein; Forms pores that allow passive diffusion of small molecules across the outer membrane; Belongs to the Gram-negative porin family. (362 aa)
ompAPutative membrane component hydrogenase; With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. (350 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
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