Proteins

Genome: KpKP13

Description: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence

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5192 / 5842 proteins Structure: AlphaFold

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# Protein Description Gene Structure EC GO Metabolism 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.
2701 KP13_02549 hypothetical protein AlphaFold DB model + ColabFold model – – No map 0.54 No Hit 0.0% —
2702 KP13_20435 7-cyano-7-deazaguanine synthase queC AlphaFold DB model + ColabFold model
6.3.4.20
GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0016879Catalysis of the joining of two molecules, or two groups within a single molecule, via a carbon-nitrogen bond, with the concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate. GO:0008270Binding to a zinc ion (Zn). +14 total
No map 0.539 No Hit 0.0% —
2703 KP13_04757 hypothetical protein AlphaFold DB model + ColabFold model – – No map 0.539 No Hit 0.0% —
2704 KP13_04172 N-carbamoyl-L-amino acid hydrolase amaB AlphaFold DB model + ColabFold model –
GO:0016813Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a linear amidine, a compound of the form R-C(=NH)-NH2. GO:0016787Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. GO:0046872Binding to a metal ion.
No map 0.539 No Hit 0.0% —
2705 KP13_03986 hypothetical protein AlphaFold DB model + ColabFold model – – No map 0.539 No Hit 0.0% —
2706 KP13_03355 Universal stress protein G AlphaFold DB model + ColabFold model – – No map 0.539 No Hit 0.0% —
2707 KP13_02539 Fic domain-containing protein AlphaFold DB model + ColabFold model
2.7.7.-
GO:0016779Catalysis of the transfer of a nucleotidyl group from one compound (donor) to another (acceptor).
No map 0.539 Hit 26.0% 1.67e-09
2708 KP13_31789 DUF336 family protein AlphaFold DB model + ColabFold model – – No map 0.538 No Hit 0.0% —
2709 KP13_06820 conjugal transfer TrbM-like protein trbM AlphaFold DB model + ColabFold model – – No map 0.538 No Hit 0.0% —
2710 KP13_05349 Ribosomal large subunit pseudouridine synthase B rluB AlphaFold DB model + ColabFold model
5.4.99.-
GO:0009451The covalent alteration of one or more nucleotides within an RNA molecule to produce an RNA molecule with a sequence that differs from that coded genetically. GO:0009982Catalysis of the reaction: a uridine in RNA = a pseudouridine in RNA. Conversion of uridine in an RNA molecule to pseudouridine by rotation of the C1'-N-1 glycosidic bond of uridine in RNA to a C1'-C5. GO:0001522The intramolecular conversion of uridine to pseudouridine within an RNA molecule. +47 total
No map 0.538 No Hit 0.0% —
2711 KP13_04725 Leu/Ile/Val-binding protein AlphaFold DB model + ColabFold model –
GO:0006865The directed movement of amino acids, organic acids containing one or more amino substituents, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. 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:0015820The directed movement of L-leucine, 2-amino-4-methylpentanoic acid, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
No map 0.538 No Hit 0.0% —
2712 KP13_04441 Protocatechuate 3,4-dioxygenase alpha chain AlphaFold DB model + ColabFold model –
GO:0016702Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from one donor, and two oxygen atoms is incorporated into a donor. GO:0018578Catalysis of the reaction: 3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate. GO:0019439OBSOLETE. The chemical reactions and pathways resulting in the breakdown of aromatic compounds, any substance containing an aromatic carbon ring. +47 total
No map 0.538 No Hit 0.0% —
2713 KP13_04393 ATP-dependent DNA helicase AlphaFold DB model + ColabFold model –
GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0003677Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). GO:0016787Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. +36 total
No map 0.538 No Hit 0.0% —
2714 KP13_04085 Metal-dependent phosphohydrolase AlphaFold DB model + ColabFold model – – No map 0.538 No Hit 0.0% —
2715 KP13_03140 Deoxycytidine triphosphate deaminase dcd AlphaFold DB model + ColabFold model
3.5.4.13
GO:0006229The chemical reactions and pathways resulting in the formation of dUTP, deoxyuridine (5'-)triphosphate. GO:0008829Catalysis of the reaction: dCTP + H2O + H+ = dUTP + NH4+. GO:0000166Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose. +25 total
No map 0.538 No Hit 0.0% —
2716 KP13_02358 putative exonuclease xni xni AlphaFold DB model + ColabFold model
3.1.-.-
GO:0017108Catalysis of the cleavage of a 5' flap structure in DNA, but not other DNA structures; processes the 5' ends of Okazaki fragments in lagging strand DNA synthesis. GO:0048256Catalysis of the cleavage of a flap structure in DNA, but not other DNA structures; processes the ends of Okazaki fragments in lagging strand DNA synthesis. GO:0033567The DNA metabolic process, occurring during lagging strand synthesis, by which RNA primers are removed from Okazaki fragments, the resulting gaps filled by DNA polymerization, and the ends ligated to form a continuous strand. +58 total
No map 0.538 No Hit 0.0% —
2717 KP13_01381 Sensor protein zraS zraS AlphaFold DB model + ColabFold model
2.7.13.3
GO:0016310The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide. 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. 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. +36 total
No map 0.538 No Hit 0.0% —
2718 KP13_00662 Aspartate-semialdehyde dehydrogenase asd AlphaFold DB model + ColabFold model –
GO:0009089OBSOLETE. The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate. GO:0009086OBSOLETE. The chemical reactions and pathways resulting in the de novo formation of L-methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins. GO:0009097OBSOLETE. The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid. +811 total
No map 0.538 No Hit 0.0% —
2719 KP13_00493 10 kDa chaperonin groS AlphaFold DB model + ColabFold model –
GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0044183Binding to a protein or a protein-containing complex to assist the protein folding process. GO:0006457The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
No map 0.538 Hit 41.4% 5.70e-08
2720 KP13_31625 Transcriptional activator rfaH rfaH AlphaFold DB model + ColabFold model –
GO:0140673A chromatin remodeling process that reestablishes the chromatin structure following the passage of RNA polymerase II during transcription elongation, thus preventing cryptic transcription initiation. GO:0006355Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription. GO:0005829The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. +36 total
No map 0.537 No Hit 0.0% —
2721 KP13_06845 hypothetical protein AlphaFold DB model + ColabFold model – – No map 0.537 No Hit 0.0% —
2722 KP13_03822 Putative peroxiredoxin bcp bcp AlphaFold DB model + ColabFold model
1.11.1.24
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. GO:0016209Inhibition of the reactions brought about by dioxygen (O2) or peroxides. Usually the antioxidant is effective because it can itself be more easily oxidized than the substance protected. The term is often applied to components that can trap free radicals, thereby breaking the chain reaction that normally leads to extensive biological damage. GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. +36 total
No map 0.537 Hit 30.7% 3.80e-10
2723 KP13_01614 Pyruvate kinase II pykA AlphaFold DB model + ColabFold model
2.7.1.40
GO:0030955Binding to a potassium ion (K+). GO:0000287Binding to a magnesium (Mg) ion. 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. +47 total
No map 0.537 Hit 50.0% 5.61e-06
2724 KP13_31940 Formate acetyltransferase pfl AlphaFold DB model + ColabFold model
2.3.1.54
GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0008861Catalysis of the reaction: acetyl-CoA + formate = CoA + pyruvate. 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. +36 total
No map 0.536 No Hit 0.0% —
2725 KP13_31620 Starvation-sensing protein rspB rspB AlphaFold DB model + ColabFold model –
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. GO:0008270Binding to a zinc ion (Zn).
No map 0.536 Hit 41.5% 8.97e-12
Page of 208 · 5192 total proteins