Proteins

Genome: KpKP13

Description: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence

Search, filter, and prioritize proteins.

Export view
5842 proteins

Scoring formula None

Sorted by Druggability (descending)

Applied filters No active filters

Search query No active search

Rows per page 25

Rows
# 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.
4226 KP13_31751 hypothetical protein ColabFold – – 0.356 No Hit 0.0% —
4227 KP13_04223 ATP-dependent Clp protease adapter protein clpS clpS AlphaFold + ColabFold –
GO:0030163The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. GO:0006508The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. 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.
0.356 No Hit 0.0% —
4228 KP13_03845 Ethanolamine utilization protein eutD eutD AlphaFold + ColabFold
2.3.1.8
GO:0016407Catalysis of the transfer of an acetyl group to an acceptor molecule. GO:0016746Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor). GO:0008959Catalysis of the reaction: acetyl-CoA + phosphate = CoA + acetyl phosphate.
0.356 No Hit 0.0% —
4229 KP13_03162 Phosphatase AlphaFold + ColabFold –
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.
0.356 No Hit 0.0% —
4230 KP13_02918 putative glycerophosphoryl diester phosphodiesterase AlphaFold + ColabFold –
GO:0008081Catalysis of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group. GO:0006629The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
0.356 Hit 39.4% 4.49e-11
4231 KP13_02553 Iron transport system periplasmic binding component SitA sitA AlphaFold + ColabFold –
GO:0030001The directed movement of metal ions, any metal ion with an electric charge, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. 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:0046872Binding to a metal ion. +14 total
0.356 No Hit 0.0% —
4232 KP13_02412 Ribosome-associated inhibitor A raiA AlphaFold + ColabFold –
GO:0044238The chemical reactions and pathways involving those compounds which are formed as a part of the normal anabolic and catabolic processes. These processes take place in most, if not all, cells of the organism. GO:0022627The small subunit of a ribosome located in the cytosol. GO:0043024Binding to a small ribosomal subunit. +14 total
0.356 No Hit 0.0% —
4233 KP13_02362 putative monooxygenase AlphaFold + ColabFold –
GO:0004497Catalysis of the incorporation of one atom of molecular oxygen (O2) into the substrate and the reduction of the other atom of O2 to water. GO:0016705Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from each of two donors, and molecular oxygen is reduced or incorporated into a donor.
0.356 No Hit 0.0% —
4234 KP13_01180 Phosphoribosyl-dephospho-CoA transferase mdcG ColabFold –
GO:0016779Catalysis of the transfer of a nucleotidyl group from one compound (donor) to another (acceptor).
0.356 No Hit 0.0% —
4235 KP13_00502 FimC-like chaperone protein AlphaFold + ColabFold –
GO:0061077OBSOLETE. The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone. GO:0043711A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a pilus, a short filamentous structure on a bacterial cell, flagella-like in structure and generally present in many copies. 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. +14 total
0.356 No Hit 0.0% —
4236 KP13_32142 hypothetical protein ColabFold – – 0.355 No Hit 0.0% —
4237 KP13_10157 50S ribosomal protein L14 rplN 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
0.355 Hit 41.9% 1.54e-13
4238 KP13_05391 Osmotically-inducible lipoprotein E osmE AlphaFold + ColabFold –
GO:0019867The external membrane of Gram-negative bacteria or certain organelles such as mitochondria and chloroplasts; freely permeable to most ions and metabolites.
0.355 No Hit 0.0% —
4239 KP13_04879 hypothetical protein ColabFold – – 0.355 No Hit 0.0% —
4240 KP13_03878 Methylglyoxal synthase mgsA AlphaFold + ColabFold
4.2.3.3
GO:0008929Catalysis of the reaction: glycerone phosphate = methylglyoxal + phosphate. GO:0019242The chemical reactions and pathways resulting in the formation of methylglyoxal, CH3-CO-CHO, the aldehyde of pyruvic acid. GO:0005829The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
0.355 No Hit 0.0% —
4241 KP13_01658 hypothetical protein AlphaFold + ColabFold – – 0.355 No Hit 0.0% —
4242 KP13_00958 Ribonucleoside-diphosphate reductase 1 subunit alpha nrdA AlphaFold + ColabFold
1.17.4.1
GO:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. 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:0004748Catalysis of the reaction: 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin. Thioredoxin disulfide is the oxidized form of thioredoxin. +25 total
0.354 Hit 27.6% 6.44e-51
4243 KP13_32111 putative replication initiation protein ColabFold – – 0.352 No Hit 0.0% —
4244 KP13_09671 sn-glycerol-3-phosphate import ATP-binding protein ugpC AlphaFold + ColabFold –
GO:0008643The directed movement of carbohydrate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Carbohydrates are a group of organic compounds based of the general formula Cx(H2O)y. 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:0005524Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. +47 total
0.352 Hit 51.3% 6.51e-06
4245 KP13_06652 hypothetical protein ColabFold – – 0.352 No Hit 0.0% —
4246 KP13_05761 hypothetical protein ColabFold – – 0.352 No Hit 0.0% —
4247 KP13_04971 putative phenylacetic acid degradation NADH oxidoreductase paaE paaE 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: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:0010124The chemical reactions and pathways resulting in the breakdown of phenylacetate. +36 total
0.352 Hit 26.7% 1.63e-09
4248 KP13_04779 hypothetical protein AlphaFold + ColabFold – – 0.352 No Hit 0.0% —
4249 KP13_02337 Cobalt transport protein cbiN cbiN AlphaFold + ColabFold –
GO:0006824The directed movement of cobalt (Co2+) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. GO:0015087Enables the transfer of cobalt (Co2+) ions from one side of a membrane to the other. GO:0009236The chemical reactions and pathways resulting in the formation of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom. +25 total
0.352 No Hit 0.0% —
4250 KP13_02026 DNA polymerase III subunit psi holD 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:0008408Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' end.
0.352 No Hit 0.0% —
Page of 234 · 5842 total proteins