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fepB fepB fepD fepD fepC fepC fes fes fepA fepA cusA cusA cusB cusB cusF cusF cusC cusC cusR cusR cusS cusS cueR cueR mhpT mhpT mhpE mhpE mhpF mhpF mhpD mhpD mhpC mhpC mhpA mhpA mhpR mhpR fhuB fhuB cueO cueO entS entS nikR nikR nikD nikD nikC nikC nikB nikB nikA nikA ygiD ygiD cirA cirA ptrB ptrB sad sad ydcO ydcO paaK paaK paaJ paaJ paaZ paaZ tyrR tyrR tonB tonB moeB moeB fiu fiu moaE moaE moaD moaD moaC moaC moaB moaB fur fur mobB mobB
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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fepBFerrienterobactin ABC transporter periplasmic binding protein; Binds ferrienterobactin; part of the binding-protein- dependent transport system for uptake of ferrienterobactin. (318 aa)
fepDFerrienterobactin ABC transporter permease; Part of the binding-protein-dependent transport system for ferric enterobactin. Probably responsible for the translocation of the substrate across the membrane. (334 aa)
fepCFerrienterobactin ABC transporter ATPase; Part of the binding-protein-dependent transport system for ferric enterobactin. Probably responsible for energy coupling to the transport system. (271 aa)
fesEnterobactin/ferrienterobactin esterase; Upon internalization, ferric enterobactin is processed via an exquisitely specific pathway that is dependent on FES activity, making iron available for metabolic use; Belongs to the Fes family. (400 aa)
fepAFerrienterobactin outer membrane transporter; This protein is involved in the initial step of iron uptake by binding ferrienterobactin (Fe-ENT), an iron chelatin siderophore that allows E.coli to extract iron from the environment. FepA also acts as a receptor for colicins B and D. (746 aa)
cusACopper/silver efflux system, membrane component; Part of a cation efflux system that mediates resistance to copper and silver; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. (1047 aa)
cusBCopper/silver efflux system, membrane fusion protein; Part of a cation efflux system that mediates resistance to copper and silver. (407 aa)
cusFPeriplasmic copper- and silver-binding protein; Part of a cation efflux system that mediates resistance to copper and silver. Binds one copper per polypeptide. (110 aa)
cusCCopper/silver efflux system, outer membrane component; Forms pores that allow passive diffusion of cations across the outer membrane. Part of a cation efflux system that mediates resistance to copper and silver. In pathogenic strains it allows the bacteria to invade brain microvascular endothelial cells (BMEC) thus allowing it to cross the blood-brain barrier and cause neonatal meningitis. (457 aa)
cusRResponse regulator in two-component regulatory system with CusS; Member of the two-component regulatory system CusS/CusR involved in response to copper and silver. Activates the expression of cusCFBA, hiuH and plasmid pRJ1004 gene pcoE in response to increasing levels of copper or silver ions. Can also increase the basal-level expression of copper resistance gene operon pcoABCD. (227 aa)
cusSCopper-sensing histidine kinase in two-component regulatory system with CusR; Member of the two-component regulatory system CusS/CusR involved in response to copper and silver. Acts as a copper/silver ion sensor. Activates CusR by phosphorylation. (480 aa)
cueRCopper-responsive regulon transcriptional regulator; Regulates the transcription of the copA and cueO genes. It detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations. (135 aa)
mhpT3-hydroxyphenylpropionic transporter; Uptake of 3-(3-hydroxyphenyl)propionate (3HPP) across the cytoplasmic membrane. Transport is driven by the proton motive force. Does not transport benzoate, 3-hydroxybenzoate or gentisate. Belongs to the major facilitator superfamily. Aromatic acid:H(+) symporter (AAHS) (TC 2.A.1.15) family. (403 aa)
mhpE4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase, class I; Catalyzes the retro-aldol cleavage of 4-hydroxy-2- oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta- cleavage pathway for the degradation of 3-phenylpropanoate. Belongs to the 4-hydroxy-2-oxovalerate aldolase family. (337 aa)
mhpFacetaldehyde-CoA dehydrogenase II, NAD-binding; Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Functions as a chaperone protein for folding of MhpE. (316 aa)
mhpD2-keto-4-pentenoate hydratase; Catalyzes the conversion of 2-hydroxypentadienoic acid (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic acid. Belongs to the hydratase/decarboxylase family. MhpD subfamily. (269 aa)
mhpC2-hydroxy-6-ketonona-2,4-dienedioic acid hydrolase; Catalyzes the cleavage of the C5-C6 bond of 2-hydroxy-6- oxononadienedioate and 2-hydroxy-6-oxononatrienedioate, a dienol ring fission product of the bacterial meta-cleavage pathway for degradation of phenylpropionic acid. MhpC shows some selectivity for the carboxylate of the side chain; Belongs to the AB hydrolase superfamily. MhpC family. (288 aa)
mhpA3-(3-hydroxyphenyl)propionate hydroxylase; Catalyzes the insertion of one atom of molecular oxygen into position 2 of the phenyl ring of 3-(3-hydroxyphenyl)propionate (3-HPP) and hydroxycinnamic acid (3HCI). (554 aa)
mhpRMhp operon transcriptional activator; Activator of the mhpABCDFE operon coding for components of the 3-hydroxyphenylpropionate degradation pathway. (277 aa)
fhuBIron(3+)-hydroxamate import ABC transporter permease; Part of the ABC transporter complex FhuCDB involved in iron(3+)-hydroxamate import. Responsible for the translocation of the substrate across the membrane. (660 aa)
cueOMulticopper oxidase (laccase); Probably involved in periplasmic detoxification of copper by oxidizing Cu(+) to Cu(2+) and thus preventing its uptake into the cytoplasm. Possesses phenoloxidase and ferroxidase activities and might be involved in the production of polyphenolic compounds and the prevention of oxidative damage in the periplasm. (516 aa)
entSEnterobactin exporter, iron-regulated; Component of an export pathway for enterobactin. Overexpression reduces intracellular arabinose concentrations. (416 aa)
nikRTranscriptional repressor, Ni-binding; Transcriptional repressor of the nikABCDE operon. Is active in the presence of excessive concentrations of intracellular nickel; Belongs to the transcriptional regulatory CopG/NikR family. (133 aa)
nikDNickel ABC transporter ATPase; Part of the ABC transporter complex NikABCDE involved in nickel import. Responsible for energy coupling to the transport system. Belongs to the ABC transporter superfamily. Nickel importer (TC 3.A.1.5.3) family. (254 aa)
nikCNickel ABC transporter permease; Involved in a nickel transport system, probably translocates nickel through the bacterial inner membrane. (277 aa)
nikBNickel ABC transporter permease; Involved in a nickel transport system, probably translocates nickel through the bacterial inner membrane. (314 aa)
nikANickel/heme ABC transporter periplasmic binding protein; Involved in a nickel transport system, probably represents the nickel binder. (524 aa)
ygiD4,5- DOPA-extradiol-dioxygenase; In vitro, opens the cyclic ring of dihydroxy-phenylalanine (DOPA) between carbons 4 and 5, thus producing an unstable seco-DOPA that rearranges nonenzymatically to betalamic acid. The physiological substrate is unknown. (262 aa)
cirAColicin IA outer membrane receptor and translocator; Not yet known. Postulated to participate in iron transport. Outer membrane receptor for colicins IA and IB. (663 aa)
ptrBProtease II; Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues; Belongs to the peptidase S9A family. (686 aa)
sadSuccinate semialdehyde dehydrogenase, NAD(P)+-dependent; Catalyzes the NAD(+)-dependent oxidation of succinate semialdehyde to succinate. It acts preferentially with NAD as cosubstrate but can also use NADP. Prevents the toxic accumulation of succinate semialdehyde (SSA) and plays an important role when arginine and putrescine are used as the sole nitrogen or carbon sources. (462 aa)
ydcOBenE family inner membrane putative transporter; Putative membrane transport protein. (391 aa)
paaKphenylacetyl-CoA ligase; Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA). (437 aa)
paaJ3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase; Catalyzes the thiolytic cleavage of the beta-keto C8 intermediate 3-oxo-5,6-dehydrosuberyl-CoA with CoA to yield the C6 intermediate 2,3-dehydroadipyl-CoA and acetyl-CoA. Besides it catalyzes also the last step of the pathway, in which 3-oxoadipyl-CoA similarly is cleaved to acetyl-CoA and succinyl-CoA. Belongs to the thiolase-like superfamily. Thiolase family. (401 aa)
paaZoxepin-CoA hydrolase and 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase; Catalyzes the hydrolytic ring cleavage of 2-oxepin-2(3H)- ylideneacetyl-CoA (oxepin-CoA) via the open-chain aldehyde intermediate to yield 3-oxo-5,6-dehydrosuberyl-CoA. The enzyme consists of a C- terminal (R)-specific enoyl-CoA hydratase domain (formerly MaoC) that cleaves the ring and produces the highly reactive 3-oxo-5,6- dehydrosuberyl-CoA semialdehyde and an N-terminal NADP-dependent aldehyde dehydrogenase domain that oxidizes the aldehyde to 3-oxo-5,6- dehydrosuberyl-CoA. Can also use crotonyl-CoA [...] (681 aa)
tyrRAromatic amino acid biosynthesis and transport regulon transcriptional regulator; Involved in transcriptional regulation of aromatic amino acid biosynthesis and transport. Modulates the expression of at least 8 unlinked operons. Seven of these operons are regulated in response to changes in the concentration of the three aromatic amino acids (phenylalanine, tyrosine and tryptophan). These amino acids are suggested to act as co-effectors which bind to the TyrR protein to form an active regulatory protein. In most cases TyrR causes negative regulation, but positive effects on the tyrP ge [...] (513 aa)
tonBMembrane spanning protein in TonB-ExbB-ExbD transport complex; Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to tran [...] (239 aa)
moeBMolybdopterin synthase sulfurylase; Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein MoaD. (249 aa)
fiuCatecholate siderophore receptor; Involved in the active transport across the outer membrane of iron complexed with catecholate siderophores such as dihydroxybenzoylserine and dihydroxybenzoate. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Can also transport catechol-substituted cephalosporins. Receptor for microcins M, H47 and E492. (760 aa)
moaEMolybdopterin synthase, large subunit; Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD. (150 aa)
moaDMolybdopterin synthase, small subunit; Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin. Belongs to the MoaD family. (81 aa)
moaCMolybdopterin biosynthesis, protein C; Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP). (161 aa)
moaBInactive molybdopterin adenylyltransferase; May be involved in the biosynthesis of molybdopterin. Can bind GTP and has low GTPase activity. Can bind MPT, but has no MPT adenylyl transferase activity; Belongs to the MoaB/Mog family. (170 aa)
furFerric iron uptake regulon transcriptional repressor; Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes. Regulates the expression of several outer-membrane proteins including the iron transport operon; Belongs to the Fur family. (148 aa)
mobBMolybdopterin-guanine dinucleotide biosynthesis protein B; GTP-binding protein that is not required for the biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not necessary for the formation of active molybdoenzymes using this form of molybdenum cofactor. May act as an adapter protein to achieve the efficient biosynthesis and utilization of MGD. Displays a weak intrinsic GTPase activity. Is also able to bind the nucleotides ATP, TTP and GDP, but with lower affinity than GTP. (175 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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