dbACP: A Comprehensive Database of Anti-Cancer Peptides

dbacp04682

General Description

Peptide name : Microcin E492

Source/Organism : Human microbiota:gut, symbiont bacteria

Linear/Cyclic : Not found

Chirality : L

Sequence Information

Sequence : GETDPNTQLLNDLGNnMAWGAALGAPGGLGSAALGAAGGALQTVGQGLIDHGPVNVFIPVLIGPSWNGSGSGYNSATSSSGSGS

Peptide length: 84

C-terminal modification: Not found

N-terminal modification : Free

Non-natural peptide information: None

Activity Information

Assay type : Not specified

Assay time : Not found

Activity : Not found

Cell line : Not found

Cancer type : Not found

Other activity : Not found

Physicochemical Properties

Amino acid composition bar chart :

Molecular mass : 7936.5329 Dalton

Aliphatic index : 0.814

Instability index : 18.9131

Hydrophobicity (GRAVY) : 0.0655

Isoelectric point : 4.05

Charge (pH 7) : -4.1476

Aromaticity : 0.047

Molar extinction coefficient (cysteine, cystine): (12490, 12490)

Hydrophobic/hydrophilic ratio : 1.86206896

hydrophobic moment : 0.0166

Missing amino acid : C,K,R

Most occurring amino acid : G

Most occurring amino acid frequency : 19

Least occurring amino acid : E

Least occurring amino acid frequency : 1

Structural Information

3D structure :

Secondary structure fraction (Helix, Turn, Sheet): (0.2, 0.5, 0.2)

SMILES Notation: CC[C@H](C)[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)CNC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](C)NC(=O)[C@H](CCSC)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(=O)O)NC(=O)[C@@H](NC(=O)[C@H](CCC(=O)O)NC(=O)CN)[C@@H](C)O)[C@@H](C)O)[C@@H](C)O)C(C)C)[C@@H](C)CC)C(C)C)C(C)C)[C@@H](C)CC)C(C)C)C(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CO)C(=O)O)[C@@H](C)O

Secondary Structure :

Method Prediction
GOR CCCCCCCEEEETTTCCHHHHHHTTCCTCCCEEEEHHHCCEEEEEEEEEEETCCCCEEEEEEECCCEETTTEEEEEEEEETTTCC
Chou-Fasman (CF) CCCCCEECCCCCCCHHHHHHHHCCCCCCHHHHHHHHHCCCEEEECEECCCCCEEEEEEEEEECCCCCCCCCCCCEEECCCCCCC
Neural Network (NN) CCCCCCCCCHHCCCCCCHHHHCCCCCCCCCCCHHHHCCCCCHHCCCCCCCCCCCCCCEEEECCCCCCCCCCCEEEEECCCCCCC
Joint/Consensus CCCCCCCCCCCCCCCCHHHHHHCCCCCCCCCCHHHHHCCCEEEEEEECCCCCCCCEEEEEEECCCCCCCCCCEEEEECCCCCCC

Molecular Descriptors and ADMET Properties

Molecular Descriptors: Click here to download

ADMET Properties: Click here to download

Cross Referencing databases

Pubmed Id : 6385903

Uniprot : Not available

PDB : Not available

CancerPPD : Not available

ApIAPDB : Click Here

CancerPPD2 ID : Not available

Reference

1 : de Lorenzo V. Isolation and characterization of microcin E492 from Klebsiella pneumoniae. Arch Microbiol. 1984; 139:72-5. doi: 10.1007/BF00692715

Literature

Paper title : Isolation and characterization of microcin E492 from Klebsiella pneumoniae.

Doi : https://doi.org/10.1007/BF00692715

Abstract : The production of a dialyzable peptidic antibacterial named microcin E492 by the strain of faecal origin Klebsiella pneumoniae RYC492 has previously been reported. In this paper, a procedure to extract this antibiotic from liquid cultures of the producer strain is described. This method was based in the quantitative retention of the microcin on the hydrophobic matrix Bondapak C18 and led to highly active pigment- and salt-free concentrates appropriate for further purification by high pressure liquid chromatography. The characterization of purified preparations indicated that microcin E492 was a basic and hydrophobic peptide with an apparent molecular mass of about 5,000, acid- and heat-resistant and much more active in minimal than in rich medium. These properties are discussed with regard to the likely ecological role of the microcin in the microbial ecosystem of the intestine.