Proteins

Genome: NC_002516.2

Description: Pseudomonas aeruginosa PAO1, complete genome

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5572 / 5572 proteins

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# Protein Description Gene Structure EC GO Druggability FPocket druggability score for the preferred structure (0–1): experimental structure when available, otherwise predicted model. ≥ 0.7 highly druggable · ≥ 0.4 moderately druggable · < 0.4 low druggability. Human off-target BLASTP against the human proteome. Hit means at least one human match was detected at e-value <= 1e-5. Prefer No hit for pathogen-selective targets. Human identity (%) Best human BLAST identity percentage. Human E-value Best human BLAST E-value.
2526 PA4520 chemotaxis transducer PA4520 AlphaFold –
GO:0005886The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. GO:0006935The directed movement of a motile cell or organism, or the directed growth of a cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis). GO:0007165The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. +14 total
0.756 No Hit N/A —
2527 PA4362 hypothetical protein PA4362 AlphaFold –
GO:0016491Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
0.756 Hit 28.6% 1.11e-14
2528 PA3909 extracelullar DNA degradation protein EddB eddB, PA3909 AlphaFold –
GO:0004536Catalysis of the cleavage of ester linkages within deoxyribonucleic acid. GO:0006308The cellular DNA metabolic process resulting in the breakdown of DNA, deoxyribonucleic acid, one of the two main types of nucleic acid, consisting of a long unbranched macromolecule formed from one or two strands of linked deoxyribonucleotides, the 3'-phosphate group of each constituent deoxyribonucleotide being joined in 3',5'-phosphodiester linkage to the 5'-hydroxyl group of the deoxyribose moiety of the next one. GO:0003824Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
0.756 No Hit N/A —
2529 PA3271 two-component sensor PA3271 AlphaFold
2.7.13.3
GO:0005886The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. GO:0009927Serves as a phospho-His intermediate enabling the transfer of phospho group between a hybrid kinase and a response regulator. GO:0000155Catalysis of the phosphorylation of a histidine residue in response to detection of an extracellular signal such as a chemical ligand or change in environment, to initiate a change in cell state or activity. The two-component sensor is a histidine kinase that autophosphorylates a histidine residue in its active site. The phosphate is then transferred to an aspartate residue in a downstream response regulator, to trigger a response. +811 total
0.756 No Hit N/A —
2530 PA3050 dihydroorotate dehydrogenase pyrD, PA3050 AlphaFold
1.3.5.2
GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005886The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. GO:0106430(S)-dihydroorotate + a quinone = orotate + a quinol. +710 total
0.756 Hit 50.4% 6.37e-35
2531 PA2632 hypothetical protein PA2632 AlphaFold – – 0.756 No Hit N/A —
2532 PA2081 kynurenine formamidase KynB kynB, PA2081 Experimental + AlphaFold
3.5.1.9
GO:0004061Catalysis of the reaction: N-formyl-L-kynurenine + H2O = formate + L-kynurenine. GO:0004328Catalysis of the reaction: formamide + H2O = formate + NH4. GO:0008270Binding to a zinc ion (Zn). +25 total
0.756 No Hit N/A —
2533 PA1408 hypothetical protein PA1408 AlphaFold –
GO:0005886The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. GO:0008381Enables the transmembrane transfer of an monoatomic ion by a channel that opens in response to a mechanical stress. GO:0055085The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other. +14 total
0.756 No Hit N/A —
2534 PA1112a hypothetical protein ColabFold –
GO:0003677Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
0.756 No Hit N/A —
2535 PA0974 hypothetical protein cpoB, PA0974 AlphaFold –
GO:0030288The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall. GO:0043093A cytokinesis process that involves a set of conserved proteins including FtsZ, and results in the formation of two similarly sized and shaped cells. GO:0070206The formation of a protein trimer, a macromolecular structure consisting of three noncovalently associated identical or nonidentical subunits. +25 total
0.756 No Hit N/A —
2536 PA0669 error-prone DNA polymerase PA0669, dnaE2 ColabFold
2.7.7.7
GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0008408Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end. GO:0003887Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. +58 total
0.756 No Hit N/A —
2537 PA0063 hypothetical protein PA0063 AlphaFold – – 0.756 No Hit N/A —
2538 PA5422 hypothetical protein PA5422 AlphaFold
5.1.3.15
GO:0030246Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates. GO:0047938Catalysis of the reaction: alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate. GO:0008976Catalysis of the reaction: ATP + phosphate(n) = ADP + phosphate(n+1). +47 total
0.755 No Hit N/A —
2539 PA5166 two-component response regulator PA5166, dctD AlphaFold –
GO:0032993A macromolecular complex containing both protein and DNA molecules. GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0000987Binding to a specific upstream regulatory DNA sequence (transcription factor recognition sequence or binding site, located in cis relative to the transcription start site (i.e., on the same strand of DNA) of a gene transcribed by some RNA polymerase. Cis-regulatory sites are often referred to as a sequence motifs, enhancers, or silencers. +912 total
0.755 No Hit N/A —
2540 PA5156 hypothetical protein ColabFold – – 0.755 No Hit N/A —
2541 PA5108 hypothetical protein PA5108 AlphaFold –
GO:0019867The external membrane of Gram-negative bacteria or certain organelles such as mitochondria and chloroplasts; freely permeable to most ions and metabolites.
0.755 No Hit N/A —
2542 PA4472 PmbA protein pmbA, PA4472 Experimental + AlphaFold –
GO:0005829The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:1905368A protein complex which is capable of peptidase activity. GO:0008237Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. +25 total
0.755 No Hit N/A —
2543 PA4440 hypothetical protein PA4440 AlphaFold –
GO:0009058A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
0.755 No Hit N/A —
2544 PA4348 hypothetical protein PA4348 AlphaFold – – 0.755 No Hit N/A —
2545 PA3918 molybdenum cofactor biosynthesis protein MoaC moaC, PA3918 AlphaFold
4.6.1.17
GO:0061799Catalysis of the reaction: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate. GO:0006777The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands.
0.755 Hit 51.9% 1.35e-45
2546 PA3290 hypothetical protein PA3290 Experimental + AlphaFold – – 0.755 No Hit N/A —
2547 PA2467 anti-sigma factor FoxR PA2467, foxR AlphaFold –
GO:0016989The function of binding to a sigma factor and stopping, preventing or reducing the rate of its transcriptional activity. GO:0034756Any process that modulates the frequency, rate or extent of the directed movement of iron ions (Fe) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
0.755 No Hit N/A —
2548 PA1020 acyl-CoA dehydrogenase PA1020 AlphaFold –
GO:0003995Catalysis of the reaction: a 2,3-saturated acyl-CoA + H+ oxidized [electron-transfer flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]. GO:0050660Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. GO:0016627Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
0.755 Hit 34.1% 6.85e-15
2549 PA0837 peptidyl-prolyl cis-trans isomerase SlyD PA0837, slyD AlphaFold
5.2.1.8
GO:0005829The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0003755Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0). GO:0042026The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.
0.755 No Hit N/A —
2550 PA0586 hypothetical protein PA0586 AlphaFold – – 0.755 No Hit N/A —
Page of 223 · 5572 total proteins