STRINGSTRING
metN metN yafQ yafQ dinJ dinJ cyoA cyoA sfmC sfmC umuD umuD umuC umuC dhaL dhaL btuD btuD btuC btuC secY secY ilvN ilvN ilvB ilvB atpG atpG atpH atpH atpF atpF atpE atpE btuB btuB rpoB rpoB rpoC rpoC fimC fimC panC panC panB panB btuF btuF metQ metQ
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.
Node Color
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:
metNDL-methionine transporter subunit; Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system. It has also been shown to be involved in formyl-L-methionine transport. Belongs to the ABC transporter superfamily. Methionine importer (TC 3.A.1.24) family. (343 aa)
yafQmRNA interferase toxin of toxin-antitoxin pair YafQ/DinJ; Toxic component of a type II toxin-antitoxin (TA) system. A sequence-specific mRNA endoribonuclease that inhibits translation elongation and induces bacterial stasis. Cleavage occurs between the second and third residue of the Lys codon followed by a G or A (5'AAA(G/A)3'), is reading-frame dependent and occurs within the 5' end of most mRNAs. Ribosome-binding confers the sequence specificity and reading frame- dependence. When overexpressed in liquid media YafQ partially inhibits protein synthesis, with a reduction in growth rat [...] (92 aa)
dinJAntitoxin of YafQ-DinJ toxin-antitoxin system; Antitoxin component of a type II toxin-antitoxin (TA) system. A labile antitoxin that counteracts the effect of cognate toxin YafQ. YafQ and DinJ together bind their own promoter, and repress its expression. There are 2 operators with imperfect inverted repeats (IR) in the dinJ promoter, YafQ-(DinJ)2-YafQ only binds to the first (most upstream) of them to repress transcription; binding to a single IR is sufficient for activity in vivo and in vitro. DinJ alone is as potent a transcriptional repressor as the heterotetramer and also only need [...] (86 aa)
cyoACytochrome o ubiquinol oxidase subunit II; Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. (315 aa)
sfmCPutative periplasmic pilus chaperone; Part of the sfmACDHF fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes. (230 aa)
umuDTranslesion error-prone DNA polymerase V subunit; Involved in UV protection and mutation. Poorly processive, error-prone DNA polymerase involved in translesion repair. Essential for induced (or SOS) mutagenesis. Able to replicate DNA across DNA lesions (thymine photodimers and abasic sites, called translesion synthesis) in the presence of activated RecA; efficiency is maximal in the presence of the beta sliding-clamp and clamp-loading complex of DNA polymerase III plus single-stranded binding protein (SSB). RecA and to a lesser extent the beta clamp-complex may target Pol V to replicat [...] (139 aa)
umuCTranslesion error-prone DNA polymerase V subunit; Involved in UV protection and mutation. Poorly processive, error-prone DNA polymerase involved in translesion repair. Essential for induced (or SOS) mutagenesis. Able to replicate DNA across DNA lesions (thymine photodimers and abasic sites, translesion synthesis) in the presence of activated RecA; efficiency is maximal in the presence of the beta sliding-clamp and clamp-loading complex of DNA polymerase III plus single-stranded binding protein (SSB). RecA and to a lesser extent the beta clamp- complex may target Pol V to replication co [...] (422 aa)
dhaLDihydroxyacetone kinase, C-terminal domain; ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL- ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone bound to DhaK. DhaL acts also as coactivator of the transcription activator DhaR by binding to the sensor domain of DhaR. In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity. In the absence of dihydroxyacetone, DhaL-ADP is converted by the PT [...] (210 aa)
btuDVitamin B12 ABC transporter ATPase; Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Responsible for energy coupling to the transport system. (249 aa)
btuCVitamin B12 ABC transporter permease; Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane; Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily. (326 aa)
secYPreprotein translocase membrane subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. SecY is r [...] (443 aa)
ilvNAcetolactate synthase I, valine sensitive, small subunit. (96 aa)
ilvBAcetolactate synthase I,valine-sensitive, large subunit. (562 aa)
atpGF1 sector of membrane-bound ATP synthase, gamma subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. (287 aa)
atpHF1 sector of membrane-bound ATP synthase, delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. (177 aa)
atpFF0 sector of membrane-bound ATP synthase, subunit b; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (156 aa)
atpEF0 sector of membrane-bound ATP synthase, subunit c; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (79 aa)
btuBVitamin B12/cobalamin outer membrane transporter; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins. (614 aa)
rpoBRNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. (1342 aa)
rpoCRNA polymerase, beta prime subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. (1407 aa)
fimCPeriplasmic chaperone; Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH. (241 aa)
panCPantothenate synthetase; Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. Belongs to the pantothenate synthetase family. (283 aa)
panB3-methyl-2-oxobutanoate hydroxymethyltransferase; Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate. (264 aa)
btuFVitamin B12 ABC transporter periplasmic binding protein; Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Binds vitamin B12 and delivers it to the periplasmic surface of BtuC. (266 aa)
metQDL-methionine transporter subunit; This protein is a component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system. Belongs to the NlpA lipoprotein family. (271 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
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.