Proteins

Genome: KpKP13

Description: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence

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5842 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.
3001 KP13_31789 DUF336 family protein AlphaFold + ColabFold – – 0.538 No Hit 0.0% —
3002 KP13_06820 conjugal transfer TrbM-like protein trbM AlphaFold + ColabFold – – 0.538 No Hit 0.0% —
3003 KP13_05349 Ribosomal large subunit pseudouridine synthase B rluB AlphaFold + ColabFold
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
0.538 No Hit 0.0% —
3004 KP13_04725 Leu/Ile/Val-binding protein AlphaFold + ColabFold –
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.
0.538 No Hit 0.0% —
3005 KP13_04441 Protocatechuate 3,4-dioxygenase alpha chain AlphaFold + ColabFold –
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
0.538 No Hit 0.0% —
3006 KP13_04393 ATP-dependent DNA helicase AlphaFold + ColabFold –
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
0.538 No Hit 0.0% —
3007 KP13_04085 Metal-dependent phosphohydrolase AlphaFold + ColabFold – – 0.538 No Hit 0.0% —
3008 KP13_03140 Deoxycytidine triphosphate deaminase dcd AlphaFold + ColabFold
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
0.538 No Hit 0.0% —
3009 KP13_02358 putative exonuclease xni xni AlphaFold + ColabFold
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
0.538 No Hit 0.0% —
3010 KP13_02253 hypothetical protein ColabFold – – 0.538 No Hit 0.0% —
3011 KP13_01381 Sensor protein zraS zraS AlphaFold + ColabFold
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
0.538 No Hit 0.0% —
3012 KP13_00662 Aspartate-semialdehyde dehydrogenase asd AlphaFold + ColabFold –
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
0.538 No Hit 0.0% —
3013 KP13_00493 10 kDa chaperonin groS AlphaFold + ColabFold –
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.
0.538 Hit 41.4% 5.70e-08
3014 KP13_31625 Transcriptional activator rfaH rfaH AlphaFold + ColabFold –
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
0.537 No Hit 0.0% —
3015 KP13_06845 hypothetical protein AlphaFold + ColabFold – – 0.537 No Hit 0.0% —
3016 KP13_03822 Putative peroxiredoxin bcp bcp AlphaFold + ColabFold
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
0.537 Hit 30.7% 3.80e-10
3017 KP13_01614 Pyruvate kinase II pykA AlphaFold + ColabFold
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
0.537 Hit 50.0% 5.61e-06
3018 KP13_32158 hypothetical protein ColabFold – – 0.536 No Hit 0.0% —
3019 KP13_31940 Formate acetyltransferase pfl AlphaFold + ColabFold
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
0.536 No Hit 0.0% —
3020 KP13_31885 Adenosylmethionine-8-amino-7-oxononanoate aminotransferase bioA Experimental + ColabFold
2.6.1.62
GO:0030170Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. GO:0009102The chemical reactions and pathways resulting in the formation of biotin, cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid. GO:0004015Catalysis of the reaction: (8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = S-adenosyl-4-methylsulfanyl-2-oxobutanoate + (7R,8S)-7,8-diammoniononanoate. +36 total
0.536 Hit 29.7% 9.59e-36
3021 KP13_31620 Starvation-sensing protein rspB rspB AlphaFold + ColabFold –
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).
0.536 Hit 41.5% 8.97e-12
3022 KP13_25192 3-oxoadipate enol-lactonase 2 AlphaFold + ColabFold –
GO:0047570Catalysis of the reaction: 3-oxoadipate enol-lactone + H2O = 3-oxoadipate. GO:0042952A pathway of aromatic compound degradation by ortho-cleavage; one branch converts protocatechuate, derived from phenolic compounds, to beta-ketoadipate, and the other branch converts catechol, generated from various aromatic hydrocarbons, amino aromatics, and lignin monomers, also to beta-ketoadipate. Two additional steps accomplish the conversion of beta-ketoadipate to tricarboxylic acid cycle intermediates.
0.536 Hit 29.4% 8.02e-07
3023 KP13_04886 4-hydroxythreonine-4-phosphate dehydrogenase pdxA AlphaFold + ColabFold –
GO:0051287Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
0.536 No Hit 0.0% —
3024 KP13_04586 Coenzyme PQQ synthesis protein E pqqE AlphaFold + ColabFold
1.21.98.4
GO:0051539Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0046872Binding to a metal 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. +710 total
0.536 No Hit 0.0% —
3025 KP13_04237 NAD(P)-binding domain-containing protein AlphaFold + ColabFold – – 0.536 Hit 25.0% 2.45e-13
Page of 234 · 5842 total proteins