STRINGSTRING
djlA djlA galU galU mshA mshA ompU ompU luxS luxS luxP luxP luxQ luxQ luxO luxO luxU luxU icmF icmF dnaJ dnaJ pilC pilC pilP pilP rscS rscS galE galE hcp hcp luxI luxI luxR luxR VF_A0954 VF_A0954 sypE sypE sypG sypG
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:
djlADnaJ-like protein, membrane anchored; Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host. (283 aa)
galUGlucose-1-phosphate uridylyltransferase. (289 aa)
mshAMSHA pilin protein MshA. (154 aa)
ompUOuter membrane protein U porin OmpU. (322 aa)
luxSS-ribosylhomocysteinase, autoinducer-2 synthase protein LuxS; Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). Belongs to the LuxS family. (172 aa)
luxPPeriplasmic AI-2 binding protein LuxP. (372 aa)
luxQMembrane-bound sensor histidine kinase LuxQ. (744 aa)
luxOAutoinducer repressor protein LuxO. (476 aa)
luxUAutoinducer phosphorelay protein LuxU. (118 aa)
icmFSecretion protein IcmF. (1173 aa)
dnaJChaperone Hsp40/DnaJ, co-chaperone with DnaK; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent intera [...] (379 aa)
pilCPilus assembly protein PilC. (412 aa)
pilPPili assembly protein PilP. (172 aa)
rscSHybrid sensor kinase RscS; Activator of syp locus genes. (927 aa)
galEUDP-galactose-4-epimerase; Belongs to the NAD(P)-dependent epimerase/dehydratase family. (336 aa)
hcpHydroxylamine reductase Hcp; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. (553 aa)
luxI3-oxo-C6-HSL autoinducer synthesis protein LuxI; Required for the synthesis of OHHL (N-(3-oxohexanoyl)-L- homoserine lactone) also known as VAI or N-(beta-ketocaproyl)homoserine lactone or 3-oxo-N-(tetrahydro-2-oxo-3-furanyl)-hexanamide, an autoinducer molecule which binds to LuxR and thus acts in bioluminescence regulation. (190 aa)
luxRAutoinducer-binding transcriptional activator protein LuxR; Transcriptional activator of the bioluminescence operon. Binds to the OHHL autoinducer. (250 aa)
VF_A0954Hemolysin co-regulated protein. (172 aa)
sypETwo-component response regulator, sigma factor PP2C-like phosphatase; Syp polysaccharide locus. (505 aa)
sypGSigma-54 dependent transcriptional regulator; Syp polysaccharide locus. (500 aa)
Your Current Organism:
Aliivibrio fischeri
NCBI taxonomy Id: 312309
Other names: A. fischeri ES114, Aliivibrio fischeri ES114, Vibrio fischeri ES114, Vibrio fischeri str. ES114, Vibrio fischeri strain ES114
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