Proteins

Genome: KpKP13

Description: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence

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5192 / 5842 proteins Structure: AlphaFold

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Structure: AlphaFold ×
# 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.
4051 KP13_05251 hypothetical protein AlphaFold + ColabFold – – 0.305 No Hit 0.0% —
4052 KP13_04999 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.
0.305 No Hit 0.0% —
4053 KP13_02951 DNA-binding protein fis fis 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:0006355Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription. GO:0003677Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). +25 total
0.305 No Hit 0.0% —
4054 KP13_01482 hypothetical protein AlphaFold + ColabFold – – 0.305 No Hit 0.0% —
4055 KP13_01459 2-dehydro-3-deoxyphosphooctonate aldolase kdsA AlphaFold + ColabFold
2.5.1.55
GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. 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. GO:0008676Catalysis of the reaction: D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 8-phospho-3-deoxy-D-manno-oct-2-ulosonate + 2 H+ + phosphate. +14 total
0.305 No Hit 0.0% —
4056 KP13_31832 Sucrose-6-phosphate hydrolase cscA AlphaFold + ColabFold
3.2.1.26
GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005975The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. GO:0004553Catalysis of the hydrolysis of any O-glycosyl bond. +25 total
0.304 No Hit 0.0% —
4057 KP13_24850 Dihydroorotase pyrC AlphaFold + ColabFold –
GO:0016812Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a cyclic amide. GO:0004151Catalysis of the reaction: (S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate + H+. GO:0019856The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases. +14 total
0.304 No Hit 0.0% —
4058 KP13_12931 DNA polymerase III subunit theta holE AlphaFold + ColabFold –
GO:0006260The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA. 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. GO:0003677Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
0.304 No Hit 0.0% —
4059 KP13_04981 FMN-dependent NADH-azoreductase azoR AlphaFold + ColabFold
1.6.5.- 1.7.1.17
GO:0016655Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a quinone or a similar acceptor molecule. GO:0010181Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. GO:0009055A molecular function representing the directed movement of electrons from one molecular entity to another, typically mediated by electron carriers or acceptors, resulting in the transfer of energy and/or the reduction-oxidation (redox) transformation of chemical species. This activity is fundamental to various biological processes, including cellular respiration and photosynthesis, as well as numerous enzymatic reactions involved in metabolic pathways. +14 total
0.304 No Hit 0.0% —
4060 KP13_03955 NADH dehydrogenase-like protein AlphaFold + ColabFold
1.6.5.9
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:0006116OBSOLETE. A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADH, to the oxidized form, NAD+. GO:0003954Catalysis of the reaction: NADH + H+ + acceptor = NAD+ + reduced acceptor. +14 total
0.304 No Hit 0.0% —
4061 KP13_01622 Crossover junction endodeoxyribonuclease ruvC ruvC AlphaFold + ColabFold
3.1.21.10
GO:0004520Catalysis of the cleavage of ester linkages within deoxyribonucleic acid by creating internal breaks. GO:0003676Binding to a nucleic acid. GO:0006310Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction. +69 total
0.304 No Hit 0.0% —
4062 KP13_01579 hypothetical protein AlphaFold + ColabFold – – 0.304 No Hit 0.0% —
4063 KP13_00768 50S ribosomal protein L15 rplO AlphaFold + ColabFold –
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:0015934The larger of the two subunits of a ribosome. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). 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. +36 total
0.304 No Hit 0.0% —
4064 KP13_32153 putative lipoprotein AlphaFold + ColabFold – – 0.303 No Hit 0.0% —
4065 KP13_05617 hypothetical protein AlphaFold + ColabFold – – 0.303 No Hit 0.0% —
4066 KP13_04582 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.
0.303 No Hit 0.0% —
4067 KP13_02928 putative glutamine amidotransferase AlphaFold + ColabFold – – 0.303 No Hit 0.0% —
4068 KP13_02471 fructosamine deglycase AlphaFold + ColabFold –
GO:1901135The chemical reactions and pathways involving carbohydrate derivative. GO:0097367Binding to a carbohydrate derivative. GO:0004360Catalysis of the reaction: D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate. +36 total
0.303 Hit 22.7% 5.64e-10
4069 KP13_01656 UvrABC system protein C uvrC AlphaFold + ColabFold –
GO:0009381Catalysis of the hydrolysis of ester linkages within deoxyribonucleic acid at sites flanking regions of damaged DNA to which the Uvr ABC excinuclease complexes bind. GO:0006289A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts). GO:0005515Binding to a protein. +58 total
0.303 No Hit 0.0% —
4070 KP13_00470 putative protein-folding factor DsbA dsbA AlphaFold + ColabFold – – 0.303 No Hit 0.0% —
4071 KP13_05221 Putative outer membrane usher protein AlphaFold + ColabFold –
GO:0005515Binding to a protein. GO:0016020A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0015473A porin that acts in the assembly of fimbria together with fimbrial chaperone. +25 total
0.302 No Hit 0.0% —
4072 KP13_03541 Thiosulfate-binding protein cysP AlphaFold + ColabFold –
GO:1901681Binding to a sulfur compound. GO:0140104Directly binding to a specific ion or molecule and delivering it either to an acceptor molecule or to a specific location. GO:1902358The directed movement of sulfate across a membrane. +14 total
0.302 No Hit 0.0% —
4073 KP13_03409 Enterochelin esterase fes AlphaFold + ColabFold –
GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0005506Binding to an iron (Fe) ion. GO:0008849Catalysis of the reaction: enterobactin + 3 H2O = 3 N-23-dihydroxybenzoyl-L-serine + 3 H+. +14 total
0.302 No Hit 0.0% —
4074 KP13_03216 Stringent starvation protein B sspB AlphaFold + ColabFold –
GO:0005829The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. 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. GO:0008233Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. +25 total
0.302 No Hit 0.0% —
4075 KP13_01834 Pullulanase pulA AlphaFold + ColabFold
3.2.1.41
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:0005975The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. GO:0004553Catalysis of the hydrolysis of any O-glycosyl bond. +14 total
0.302 No Hit 0.0% —
Page of 208 · 5192 total proteins