Proteins

Genome: KpKP13

Description: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence

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5192 proteins Structure: AlphaFold

Scoring formula None

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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.
4901 KP13_04093 Long polar fimbria protein A AlphaFold + ColabFold –
GO:0007155The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules. GO:0009289A proteinaceous hair-like appendage on the surface of bacteria ranging from 2-8 nm in diameter. GO:0043709The attachment of a cell to a solid substrate, via cell adhesion molecules, during the formation of a biofilm composed of microorganisms of the same species.
0.114 No Hit 0.0% —
4902 KP13_02514 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase ispD AlphaFold + ColabFold
2.7.7.60
GO:0008299The chemical reactions and pathways resulting in the formation of an isoprenoid compound, isoprene (2-methylbuta-1,3-diene) or compounds containing or derived from linked isoprene (3-methyl-2-butenylene) residues. 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. GO:0070567Catalysis of the transfer of a cytidylyl group to an acceptor. +25 total
0.114 Hit 27.0% 3.14e-16
4903 KP13_00445 Ribose import ATP-binding protein rbsA 2 rbsA2 AlphaFold + ColabFold –
GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0016887Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. GO:0005886The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
0.114 Hit 33.1% 7.44e-12
4904 KP13_32185 hypothetical protein AlphaFold + ColabFold – – 0.113 No Hit 0.0% —
4905 KP13_04494 putative acyltransferase AlphaFold + ColabFold –
GO:0016747Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).
0.113 No Hit 0.0% —
4906 KP13_04179 putative transposase AlphaFold + ColabFold – – 0.113 No Hit 0.0% —
4907 KP13_03356 Alkyl hydroperoxide reductase subunit F ahpF 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:0008785Catalysis of the reaction: octane hydroperoxide + NADH + H+ = H2O + NAD+ + 1-octanol. 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. +69 total
0.113 No Hit 0.0% —
4908 KP13_01923 3-isopropylmalate dehydratase large subunit leuC AlphaFold + ColabFold
4.2.1.33
GO:0003861Catalysis of the reaction: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. 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:0009098The chemical reactions and pathways resulting in the formation of L-leucine, 2-amino-4-methylpentanoic acid. +25 total
0.113 Hit 26.8% 2.05e-23
4909 KP13_01185 hypothetical protein AlphaFold + ColabFold – – 0.113 No Hit 0.0% —
4910 KP13_32220 Osmotically-inducible protein Y osmY AlphaFold + ColabFold –
GO:0042597The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
0.112 No Hit 0.0% —
4911 KP13_03316 Protein nagD nagD AlphaFold + ColabFold
3.1.3.5
GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0008253Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. GO:0046872Binding to a metal ion.
0.112 Hit 41.3% 3.13e-12
4912 KP13_03157 putative oligopeptide/dipeptide ABC transporter AlphaFold + ColabFold –
GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0016887Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
0.112 Hit 42.9% 8.35e-06
4913 KP13_05310 Cytochrome c biogenesis ATP-binding export protein CcmA ccmA AlphaFold + ColabFold –
GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0016887Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. 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. +14 total
0.111 Hit 33.5% 2.27e-12
4914 KP13_00478 hypothetical protein AlphaFold + ColabFold – – 0.111 No Hit 0.0% —
4915 KP13_32060 DNA-binding plasmid partition protein KorB AlphaFold + ColabFold –
GO:0003677Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
0.11 No Hit 0.0% —
4916 KP13_16605 Modification methylase EcoRII AlphaFold + ColabFold
2.1.1.37
GO:0008168Catalysis of the transfer of a methyl group to an acceptor molecule. GO:0003886Catalysis of the reaction: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H+ + S-adenosyl-L-homocysteine. GO:0003677Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). +36 total
0.11 Hit 23.8% 4.05e-07
4917 KP13_01187 Transcriptional regulatory protein dcuR dcuR AlphaFold + ColabFold –
GO:0000160A conserved series of molecular signals found in prokaryotes and eukaryotes; involves autophosphorylation of a histidine kinase and the transfer of the phosphate group to an aspartate that then acts as a phospho-donor to response regulator proteins. 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:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. +25 total
0.11 No Hit 0.0% —
4918 KP13_05333 Putative iron compound ABC transport system periplasmic binding component AlphaFold + ColabFold –
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:1901678The directed movement of an iron coordination entity into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
0.109 No Hit 0.0% —
4919 KP13_04521 Benzoate 1,2-dioxygenase subunit beta AlphaFold + ColabFold –
GO:0006725OBSOLETE. The chemical reactions and pathways involving aromatic compounds, any organic compound characterized by one or more planar rings, each of which contains conjugated double bonds and delocalized pi electrons, as carried out by individual cells. GO:0051213Catalysis of the incorporation of both atoms of molecular oxygen (O2) into the substrate. GO:0019380The chemical reactions and pathways resulting in the breakdown of 3-phenylpropionate, the anion of phenylpropanoic acid.
0.109 No Hit 0.0% —
4920 KP13_03905 hypothetical protein AlphaFold + ColabFold – – 0.109 No Hit 0.0% —
4921 KP13_02712 FAD-dependent pyridine nucleotide-disulfide oxidoreductase family protein 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: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:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. +14 total
0.109 Hit 26.6% 1.22e-29
4922 KP13_01027 USG-1 protein usg 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. GO:0016620Catalysis of an oxidation-reduction (redox) reaction in which an aldehyde or ketone (oxo) group acts as a hydrogen or electron donor and reduces NAD or NADP. GO:0046983The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. +14 total
0.109 No Hit 0.0% —
4923 KP13_05606 hypothetical protein AlphaFold + ColabFold – – 0.108 No Hit 0.0% —
4924 KP13_03574 hypothetical protein AlphaFold + ColabFold – – 0.108 No Hit 0.0% —
4925 KP13_00793 hypothetical protein AlphaFold + ColabFold – – 0.108 No Hit 0.0% —
Page of 208 · 5192 total proteins