Proteins

Genome: KpATCC43816

Description: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome

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5081 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.
4101 VK055_2736 hypothetical protein ColabFold – – 0.285 No Hit 0.0% —
4102 VK055_1055 hypothetical protein ColabFold – – 0.285 No Hit 0.0% —
4103 VK055_4597 RNA 2'-O ribose methyltransferase substrate binding family protein AlphaFold + ColabFold –
GO:0006396Any process involved in the conversion of one or more primary RNA transcripts into one or more mature RNA molecules. GO:0008168Catalysis of the transfer of a methyl group to an acceptor molecule. GO:0003723Binding to an RNA molecule or a portion thereof. +36 total
0.284 Hit 31.9% 1.17e-09
4104 VK055_2957 plasmid stability family protein AlphaFold + ColabFold – – 0.284 No Hit 0.0% —
4105 VK055_2142 asnC family protein AlphaFold + ColabFold –
GO:0043565Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding. GO:0005829The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0006355Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription. +14 total
0.284 No Hit 0.0% —
4106 VK055_0289 putative glutathione peroxidase AlphaFold + ColabFold
1.11.1.24 1.11.1.9
GO:0006979Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. GO:0004602Catalysis of the reaction: 2 glutathione + H2O2 = oxidized glutathione + 2 H2O. GO:0140824Catalysis of the reaction: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O. +14 total
0.284 Hit 56.5% 3.37e-17
4107 VK055_4927 LYSR-type transcriptional regulator yeiE AlphaFold + ColabFold –
GO:0003700A transcription regulator activity that modulates transcription of gene sets via selective and non-covalent binding to a specific double-stranded genomic DNA sequence (sometimes referred to as a motif) within a cis-regulatory region. Regulatory regions include promoters (proximal and distal) and enhancers. Genes are transcriptional units, and include bacterial operons. GO:0006355Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription. GO:0000976Binding to a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon.
0.283 No Hit 0.0% —
4108 VK055_3978 hypothetical protein Experimental + ColabFold –
GO:0046872Binding to a metal ion.
0.283 No Hit 0.0% —
4109 VK055_2900 putative iron-sulfur cluster-binding protein AlphaFold + ColabFold
1.17.99.6
GO:0008033The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group. GO:0008616The chemical reactions and pathways resulting in the formation of queuosines, a series of nucleosides found in position 34 of tRNA and having an additional pentenyl ring added via an NH group to the methyl group of 7-methylguanosine. The pentenyl ring may carry other substituents. The wobble nucleoside of the tRNA sequence (position 34) corresponds to the first position of the anticodon. 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. +58 total
0.283 No Hit 0.0% —
4110 VK055_2460 nicotinate-nucleotide diphosphorylase nadC AlphaFold + ColabFold
2.4.2.19
GO:0016763Catalysis of the transfer of a pentosyl group from one compound (donor) to another (acceptor). GO:0009435The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD+), a coenzyme that interconverts with its reduced form, NADH, in many redox and catabolic reactions. NAD+ is derived from various sources including vitamin B3. GO:0004514Catalysis of the reaction: CO2 + diphosphate + nicotinate D-ribonucleotide = 5-phospho-alpha-D-ribose 1-diphosphate + 2 H+ + quinolinate. +25 total
0.283 Hit 38.6% 1.05e-13
4111 VK055_1373 acyl carrier protein acpP AlphaFold + ColabFold –
GO:0006633The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes. GO:0005829The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0016020A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. +47 total
0.283 Hit 51.9% 2.27e-13
4112 VK055_0984 hypothetical protein AlphaFold + ColabFold
1.5.1.3 1.5.1.50
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:0004146Catalysis of the reaction: 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+. GO:0006730The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states.
0.283 Hit 26.0% 1.95e-09
4113 VK055_0863 dihydrodipicolinate synthetase family protein AlphaFold + ColabFold –
GO:0016829Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. GO:0008840Catalysis of the reaction: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O + H+. GO:0044281The chemical reactions and pathways involving small molecules, any low molecular weight, monomeric, non-encoded molecule.
0.283 Hit 28.8% 3.78e-18
4114 VK055_4631 PRD domain protein AlphaFold + ColabFold –
GO:0006355Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
0.282 No Hit 0.0% —
4115 VK055_4148 ahpC/TSA family protein AlphaFold + ColabFold –
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: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.
0.282 No Hit 0.0% —
4116 VK055_3114 ribosomal protein L11 rplK AlphaFold + ColabFold –
GO:0003735The action of a molecule that contributes to the structural integrity of the ribosome. GO:0006412The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome. GO:0005840An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins. +25 total
0.282 Hit 51.1% 5.76e-12
4117 VK055_2970 carbon-phosphorous lyase complex subunit AlphaFold + ColabFold –
GO:0016829Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. 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:0019700The chemical reactions and pathways resulting in the breakdown of phosphonates, any organic compound containing one or more C-PO(OH)2 or C-PO(OR)2 (with R=alkyl, aryl) groups. Catabolism of phosphonic acid itself, an inorganic compound without the biochemically relevant C-P bond, is not included.
0.282 No Hit 0.0% —
4118 VK055_2404 putative general secretion pathway protein B AlphaFold + ColabFold –
GO:0015627A large protein complex, containing 12-15 subunits, that spans the cell envelope of Gram-negative bacteria and mediates the movement of proteins into the extracellular environment. The complex includes a component in the cytoplasm, an inner membrane subcomplex that reaches into the periplasmic compartment and a secretion pore in the outer membrane. Proteins using the Type II pathway are transported across the cytoplasmic membrane by the Sec or Tat complex.
0.282 No Hit 0.0% —
4119 VK055_1206 short chain dehydrogenase family protein AlphaFold + ColabFold –
GO:0016616Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
0.282 Hit 27.0% 1.04e-09
4120 VK055_0487 lactoylglutathione lyase gloA AlphaFold + ColabFold
4.4.1.5
GO:0004462Catalysis of the reaction: (R)-S-lactoylglutathione = glutathione + methylglyoxal. GO:0046872Binding to a metal ion. GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. +14 total
0.282 Hit 36.3% 1.01e-24
4121 VK055_0154 meiotically up-regulated gene 113 family protein ColabFold – – 0.282 No Hit 0.0% —
4122 VK055_0099 hypothetical protein AlphaFold + ColabFold –
GO:0005886The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
0.282 No Hit 0.0% —
4123 VK055_0828 2Fe-2S iron-sulfur cluster binding domain protein AlphaFold + ColabFold –
GO:0051537Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0051536Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms. 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. +14 total
0.281 No Hit 0.0% —
4124 VK055_4955 substrate binding domain of ABC-type glycine betaine transport system family protein AlphaFold + ColabFold –
GO:0022857Enables the transfer of a substance, usually a specific substance or a group of related substances, from one side of a membrane to the other. GO:0043190A complex for the transport of metabolites into and out of the cell, typically comprised of four domains; two membrane-associated domains and two ATP-binding domains at the intracellular face of the membrane, that form a central pore through the plasma membrane. Each of the four core domains may be encoded as a separate polypeptide or the domains can be fused in any one of a number of ways into multidomain polypeptides. In Bacteria and Archaebacteria, ABC transporters also include substrate binding proteins to bind substrate external to the cytoplasm and deliver it to the transporter. GO:0055085The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
0.28 No Hit 0.0% —
4125 VK055_4917 mannonate dehydratase uxuA2 AlphaFold + ColabFold
4.2.1.8
GO:0006064The chemical reactions and pathways resulting in the breakdown of glucuronate, any salt or ester of glucuronic acid. GO:0008927Catalysis of the reaction: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O. GO:0008198Binding to a ferrous iron ion, Fe(II). +25 total
0.28 No Hit 0.0% —
Page of 204 · 5081 total proteins