Proteins

Genome: KpATCC43816

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

Search, filter, and prioritize proteins.

Export view
5081 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.
4401 VK055_2870 hypothetical protein AlphaFold + ColabFold – – 0.218 No Hit 0.0% —
4402 VK055_2445 aconitate hydratase 2 acnB AlphaFold + ColabFold
4.2.1.3 4.2.1.99
GO:0006099A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle. 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:0003994Catalysis of the reaction: citrate = isocitrate. The reaction occurs in two steps: (1) citrate = cis-aconitate + H2O, (2) cis-aconitate + H2O = isocitrate. This reaction is the interconversion of citrate and isocitrate via the labile, enzyme-bound intermediate cis-aconitate. Water is removed from one part of the citrate molecule and added back to a different atom to form isocitrate. +58 total
0.217 No Hit 0.0% —
4403 VK055_1376 3-oxoacyl-[acyl-carrier-] synthase III family protein fabH AlphaFold + ColabFold –
GO:0004315Catalysis of the reaction: acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]. 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:0016746Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).
0.217 No Hit 0.0% —
4404 VK055_1244 ABC transporter family protein 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.
0.217 Hit 33.1% 9.39e-14
4405 VK055_0128 fadD fadD AlphaFold + ColabFold – – 0.217 Hit 42.0% 2.82e-07
4406 VK055_5187 hypothetical protein ColabFold – – 0.216 No Hit 0.0% —
4407 VK055_4612 pyridoxine 5'-phosphate synthase pdxJ AlphaFold + ColabFold
2.6.99.2
GO:0033856Catalysis of the reaction: 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = 2 H2O + H+ + phosphate + pyridoxine 5'-phosphate. GO:0008615The chemical reactions and pathways resulting in the formation of pyridoxine, 2-methyl-3-hydroxy-4,5-bis(hydroxymethyl)pyridine, one of the vitamin B6 compounds. GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. +14 total
0.216 No Hit 0.0% —
4408 VK055_3879 winged helix-turn-helix DNA-binding family protein AlphaFold + ColabFold –
GO:0003677Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
0.216 No Hit 0.0% —
4409 VK055_3764 ribosomal protein L29 rpmC 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. +14 total
0.216 No Hit 0.0% —
4410 VK055_1398 hypothetical protein AlphaFold + ColabFold – – 0.216 No Hit 0.0% —
4411 VK055_0720 hypothetical protein AlphaFold + ColabFold – – 0.216 No Hit 0.0% —
4412 VK055_0641 hypothetical protein AlphaFold + ColabFold – – 0.216 No Hit 0.0% —
4413 VK055_0430 lysR substrate binding domain protein ColabFold – – 0.216 No Hit 0.0% —
4414 VK055_4871 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.
0.215 No Hit 0.0% —
4415 VK055_1873 tatE ybeC AlphaFold + ColabFold –
GO:0016020A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0015031The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. GO:0043953The process in which folded proteins are transported across cytoplasmic membranes of bacteria and membranes of organelles derived from bacteria (chloroplasts and mitochondria) by the TAT complex. +25 total
0.215 No Hit 0.0% —
4416 VK055_4170 putative lipoprotein; predicted DNA-binding transcriptional regulator AlphaFold + ColabFold –
GO:0032153The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles. GO:0009279A lipid bilayer that forms the outermost membrane of the cell envelope; enriched in polysaccharide and protein; the outer leaflet of the membrane contains specific lipopolysaccharide structures. GO:0005886The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. +14 total
0.214 No Hit 0.0% —
4417 VK055_2731 transposase family protein AlphaFold + ColabFold –
GO:0006313A type of transposition in which a transposable element (transposon) is moved to another part of a genome, either by a cut-and-paste mechanism or a replicative mechanism. GO:0004803Catalysis of the transposition of transposable elements or transposons. Transposases are involved in recombination required for transposition and are site-specific for the transposon/transposable element. GO:0003677Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
0.214 No Hit 0.0% —
4418 VK055_0930 metallocarboxypeptidase mcar-1 AlphaFold + ColabFold
3.4.17.19
GO:0004181Catalysis of the hydrolysis of a single C-terminal amino acid residue from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. GO:0006508The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. GO:0008270Binding to a zinc ion (Zn).
0.214 No Hit 0.0% —
4419 VK055_2436 hypothetical protein AlphaFold + ColabFold – – 0.213 No Hit 0.0% —
4420 VK055_4278 acetyltransferase family protein AlphaFold + ColabFold –
GO:0016747Catalysis of the transfer of an acyl group, other than amino-acyl, from one compound (donor) to another (acceptor).
0.212 No Hit 0.0% —
4421 VK055_3449 &alpha-xylosidase AlphaFold + ColabFold
3.2.1.177
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: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:0004553Catalysis of the hydrolysis of any O-glycosyl bond. +25 total
0.212 Hit 29.8% 9.09e-42
4422 VK055_2361 putative-tRNA hydrolase domain protein AlphaFold + ColabFold
3.1.1.29
GO:0006415The process resulting in the release of a polypeptide chain from the ribosome, usually in response to a termination codon (UAA, UAG, or UGA in the universal genetic code). GO:0003747Involved in catalyzing the release of a nascent polypeptide chain from a ribosome. GO:0005737The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. +47 total
0.212 No Hit 0.0% —
4423 VK055_2004 hypothetical protein AlphaFold + ColabFold –
GO:0005515Binding to a protein.
0.212 No Hit 0.0% —
4424 VK055_0934 trypsin family protein AlphaFold + ColabFold
3.4.21.-
GO:0008236Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). GO:0004252Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). GO:0006508The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
0.212 No Hit 0.0% —
4425 VK055_0319 feS assembly scaffold SufA sufA AlphaFold + ColabFold –
GO:0016226The incorporation of iron and exogenous sulfur into a metallo-sulfur cluster. GO:0051536Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms. GO:0005829The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. +14 total
0.212 Hit 37.7% 9.33e-25
Page of 204 · 5081 total proteins