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bioA bioA birA birA lldP lldP bioD bioD hsdS hsdS php php luxS luxS mntH mntH glpT glpT fliY fliY yecC yecC narK narK appA appA argF argF bioF bioF
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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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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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bioA7,8-diaminopelargonic acid synthase, PLP-dependent; Catalyzes the transfer of the alpha-amino group from S- adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily. (429 aa)
birABifunctional ligase/repressor BirA; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. (321 aa)
lldPL-lactate permease; Transports L-lactate across the membrane. Can also transport D-lactate and glycolate. Seems to be driven by a proton motive force. (551 aa)
bioDDethiobiotin synthetase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring. Only CTP can partially replace ATP while diaminobiotin is only 37% as effective as 7,8-diaminopelargonic acid; Belongs to the dethiobiotin synthetase family. (225 aa)
hsdSSpecificity determinant for hsdM and hsdR; The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance M [...] (464 aa)
phpPhosphotriesterase homology protein; Its real enzymatic activity is not yet known. It was tested for general esterase, aminopeptidase, sulfatase, phosphatase, carbonic anhydrase, phosphodiesterase, and phosphotriesterase activities with the following substrates: p-nitrophenyl acetate, L-alanine nitroanilide, p-nitrophenyl sulfate, bis(p-nitrophenyl) phosphate, paraoxon, and p-nitrophenyl phosphate. No enzymatic activity was detected with any of these non-specific substrates. (292 aa)
luxSS-ribosylhomocysteine lyase; 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. (171 aa)
mntHManganese/divalent cation transporter; H(+)-stimulated, divalent metal cation uptake system. Involved in manganese and iron uptake. Can also transport cadmium, cobalt, zinc and to a lesser extent nickel and copper. Involved in response to reactive oxygen. (412 aa)
glpTSn-glycerol-3-phosphate transporter; Responsible for glycerol-3-phosphate uptake. (452 aa)
fliYCystine transporter subunit; Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L- cysteine, and it mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Binds cystine ; Belongs to the bacterial solute-binding protein 3 family. (266 aa)
yecCPutative ABC transporter ATPase; Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L- cysteine, and it mediates accumulation of the toxic compounds L- selenaproline (SCA) and L-selenocystine (SeCys). Probably responsible for energy coupling to the transport system (Probable). (250 aa)
narKNitrate/nitrite transporter; Catalyzes nitrate uptake, nitrite uptake and nitrite export across the cytoplasmic membrane. Functions as a nitrate/nitrite exchanger, and protons are probably not co-transported with the substrate. (463 aa)
appAPhosphoanhydride phosphorylase; pH 2.5 acid phosphatase; periplasmic; Protein involved in phosphorus metabolic process and response to starvation. (432 aa)
argFOrnithine carbamoyltransferase 2, chain F; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis. (334 aa)
bioF8-amino-7-oxononanoate synthase; Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. Can also use pimeloyl-CoA instead of pimeloyl-ACP as substrate, but it is believed that pimeloyl- ACP rather than pimeloyl-CoA is the physiological substrate of BioF. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily. (384 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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