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malE malE fhuA fhuA htrA htrA phoE phoE fimH fimH ompA ompA lpp lpp fliC fliC sopA sopA ompC ompC fljB fljB degQ degQ fkpA fkpA ftsY ftsY secB secB dsbA dsbA lamB lamB
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:
malEMaltose transport protein; Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Binds maltose and higher maltodextrins. (399 aa)
fhuAIron complex outermembrane recepter protein; Similar to E. coli outer membrane protein receptor for ferrichrome, colicin M, and phages T1, T5, and phi80 (AAC73261.1); Blastp hit to AAC73261.1 (747 aa), 68% identity in aa 1 - 747. (729 aa)
htrAPeriplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] (475 aa)
phoEOuter membrane pore protein e (e,ic,nmpab); Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes; Belongs to the Gram-negative porin family. (350 aa)
fimHMinor fimbrial subunit; Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). A mannose-binding adhesin (By similarity). Belongs to the fimbrial protein family. (335 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)
lppMurein lipoprotein; Plays an important role in virulence. A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non- covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane (By similarity). (78 aa)
fliCFlagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (495 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)
ompCOuter membrane protein 1b (ib;c); Forms pores that allow passive diffusion of small molecules across the outer membrane. (378 aa)
fljBFilament structural protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (506 aa)
degQSimilar to E. coli serine endoprotease (AAC76266.1); Blastp hit to AAC76266.1 (455 aa), 89% identity in aa 1 - 455; Belongs to the peptidase S1C family. (455 aa)
fkpASimilar to E. coli FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase) (AAC76372.1); Blastp hit to AAC76372.1 (270 aa), 90% identity in aa 1 - 270. (272 aa)
ftsYGTPase domain of cell division membrane protein; Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components. (491 aa)
secBMolecular chaperone in protein export; One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA; Belongs to the SecB family. (155 aa)
dsbAPeriplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. It is required for pilus biogenesis (By similarity). Belongs to the thioredoxin family. DsbA subfamily. (207 aa)
lamBPhage lambda receptor protein; Involved in the transport of maltose and maltodextrins. Does not act as a receptor for phages; Belongs to the porin LamB (TC 1.B.3) family. (452 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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