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surA surA imp imp yacF yacF htrA htrA yaeL yaeL yaeT yaeT hlpA hlpA phoE phoE tsx tsx rlpB rlpB ybgC ybgC tolQ tolQ tolR tolR tolA tolA tolB tolB pal pal ybgF ybgF ompX ompX lolA lolA ompF ompF ycbW ycbW ompA ompA helD helD lpp lpp ompN ompN nmpC nmpC yciM yciM yciS yciS ompW ompW hns hns lolB lolB ompS ompS ompC ompC nlpB nlpB yfgL yfgL rseC rseC rseB rseB rseA rseA rpoE rpoE yfiO yfiO smpA smpA ygfE ygfE yhcB yhcB degS degS fkpA fkpA yiiU yiiU yjeP yjeP
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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
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surAPeptidyl-prolyl cis-trans isomerase; Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. (428 aa)
impOrganic solvent tolerance protein; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. (786 aa)
yacFPutative cytoplasmic protein; Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. (247 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)
yaeLPutative membrane-associated Zn-dependent protease; A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA (By similarity); Belongs to the peptidase M50B family. (450 aa)
yaeTPutative outer membrane antigen; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. (804 aa)
hlpAHistone-like protein, located in outer membrane; Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. (161 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)
tsxNucleoside channel; Functions as substrate-specific channel for nucleosides and deoxynucleosides. Functions also in albicidin uptake and as receptor for colicin K; Belongs to the nucleoside-specific channel-forming outer membrane porin (Tsx) (TC 1.B.10) family. (287 aa)
rlpBA minor lipoprotein; Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane; Belongs to the LptE lipoprotein family. (196 aa)
ybgCPutative esterase; Similar to E. coli orf, hypothetical protein (AAC73830.1); Blastp hit to AAC73830.1 (134 aa), 92% identity in aa 1 - 134. (134 aa)
tolQTol protein, membrane-spanning inner membrane protein; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. Required, with TolR, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction. (230 aa)
tolRTol protein, role in outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. Required, with TolQ, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction. (142 aa)
tolASimilar to E. coli membrane spanning protein, required for outer membrane integrity (AAC73833.1); Blastp hit to AAC73833.1 (421 aa), 70% identity in aa 1 - 420. (407 aa)
tolBTol protein required for outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. TolB occupies a key intermediary position in the Tol-Pal system because it communicates directly with both membrane-embedded components, Pal in the outer membrane and TolA in the inner membrane. (430 aa)
palTol protein required for outer membrane integrity; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. (174 aa)
ybgFPutative periplasmic protein; Mediates coordination of peptidoglycan synthesis and outer membrane constriction during cell division; Belongs to the CpoB family. (262 aa)
ompXOuter membrane protease, receptor for phage OX2; Similar to E. coli outer membrane protein X (AAC73901.1); Blastp hit to AAC73901.1 (171 aa), 91% identity in aa 1 - 171. (171 aa)
lolAPeriplasmic protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane). (204 aa)
ompFOuter membrane protein 1a (ia;b;f), porin; Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2 (By similarity). (363 aa)
ycbWPutative cytoplasmic protein; Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. (180 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)
helDDNA helicase IV; Similar to E. coli DNA helicase IV (AAC74048.1); Blastp hit to AAC74048.1 (684 aa), 83% identity in aa 1 - 684. (684 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)
ompNOuter membrane protein N; Non-specific porin; similar to E. coli putative outer membrane protein (AAC74459.1); Blastp hit to AAC74459.1 (377 aa), 81% identity in aa 1 - 377. (377 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)
yciMPutative N-acetylglucosaminyl transferase; Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane; Belongs to the LapB family. (389 aa)
yciSPutative inner membrane protein; Involved in the assembly of lipopolysaccharide (LPS). Belongs to the LapA family. (102 aa)
ompWOuter membrane protein W; Colicin S4 receptor; putative transporter; similar to E. coli putative outer membrane protein (AAC74338.1); Blastp hit to AAC74338.1 (212 aa), 88% identity in aa 1 - 212. (212 aa)
hnsDNA-binding protein HLP-II; Binds tightly to dsDNA. Acts as a global transcriptional regulator through its ability to bind to AT-rich DNA sequences. Binds in the minor groove of AT-rich DNA. Was found to bind 746 genes, about half of which show no change in expression in disruption experiments suggesting these sites are important for nucleoid structure. On a global level genes bound by H-NS are expressed at a lower than average level; H-NS is excluded from binding to highly transcribed genes and does not co-localize with RNA polymerase in DNA-binding studies during exponential growth i [...] (137 aa)
lolBOuter membrane lipoprotein; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. (207 aa)
ompSSimilar to E. coli putative outer membrane protein (AAC74459.1); Blastp hit to AAC74459.1 (377 aa), 71% identity in aa 1 - 236, 60% identity in aa 174 - 377; Belongs to the Gram-negative porin family. (398 aa)
ompCOuter membrane protein 1b (ib;c); Forms pores that allow passive diffusion of small molecules across the outer membrane. (378 aa)
nlpBLipoprotein-34; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (344 aa)
yfgLPutative serine/threonine protein kinase; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (392 aa)
rseCSimilar to E. coli sigma-E factor, negative regulatory protein (AAC75623.1); Blastp hit to AAC75623.1 (159 aa), 81% identity in aa 1 - 159. (159 aa)
rseBAnti sigma E (sigma 24) factor, negative regulator; Similar to E. coli regulates activity of sigma-E factor (AAC75624.1); Blastp hit to AAC75624.1 (318 aa), 89% identity in aa 1 - 318. (318 aa)
rseAAnti sigma E (sigma 24) factor, negative regulator; An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytop [...] (216 aa)
rpoESigma E (sigma 24) factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as acid stress, heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment (By similarity). (191 aa)
yfiOPutative lipoprotein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamA, the core component of the assembly machinery. (245 aa)
smpASmall membrane protein A; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. (112 aa)
ygfEPutative cytoplasmic protein; Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. (109 aa)
yhcBPutative periplasmic protein; Similar to E. coli orf, hypothetical protein (AAC76265.1); Blastp hit to AAC76265.1 (134 aa), 97% identity in aa 1 - 134. (134 aa)
degSPeriplasmic serine endoprotease; Similar to E. coli protease (AAC76267.1); Blastp hit to AAC76267.1 (355 aa), 91% identity in aa 1 - 355. (356 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)
yiiUPutative cytoplasmic protein; Non-essential, abundant cell division factor that is required for proper Z-ring formation. It is recruited early to the divisome by direct interaction with FtsZ, stimulating Z-ring assembly and thereby promoting cell division earlier in the cell cycle. Its recruitment to the Z-ring requires functional FtsA or ZipA. (79 aa)
yjePSimilar to E. coli putative periplasmic binding protein (AAC77119.1); Blastp hit to AAC77119.1 (1107 aa), 89% identity in aa 1 - 1107. (1108 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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