AMPDB_243 | Temporin-1Tb

1 General Description

AMPDB ID: AMPDB_243

Protein Names: Temporin-1Tb (TB) (Temporin-B)

Protein Family: Frog skin active peptide (FSAP) family; Temporin subfamily

Gene Name: Nil

Source Organism: Rana temporaria (European common frog)

Protein Length: 61 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

MFTLKKSLLLLFFLGTINLSLCEEERNAEEERRDEPDERDVQVEKRLLPIVGNLLKSLLGK

FASTA format

Counts of Amino Acids

'A': 1, 'R': 5, 'N': 3, 'D': 3, 'C': 1, 'Q': 1, 'E': 9, 'G': 3, 'H': 0, 'I': 2, 'L': 14, 'K': 5, 'M': 1, 'F': 3, 'P': 2, 'S': 3, 'T': 2, 'W': 0, 'Y': 0, 'V': 3

Frequencies of Amino Acids

'A': 1.64%, 'R': 8.2%, 'N': 4.92%, 'D': 4.92%, 'C': 1.64%, 'Q': 1.64%, 'E': 14.75%, 'G': 4.92%, 'H': 0%, 'I': 3.28%, 'L': 22.95%, 'K': 8.2%, 'M': 1.64%, 'F': 4.92%, 'P': 3.28%, 'S': 4.92%, 'T': 3.28%, 'W': 0%, 'Y': 0%, 'V': 4.92%

Missing Amino Acid(s)

H, W, Y

Most Occurring Amino Acid(s)

Less Occurring Amino Acid(s)

A, C, M, Q

Hydrophobic Amino Acid(s) Count

Hydrophilic Amino Acid(s) Count

Basic Amino Acid(s) Count

Acidic Amino Acid(s) Count

Modified Amino Acid(s) Count

Modified Amino Acid(s) Frequencies

Computed by biopython (version 1.79) & proteinAnalysis (version 1)

3 Physicochemical Properties

Sl. No.	Properties	Values	Reference
1.	Molecular Mass	7101.29 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	118.197	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	42.071	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	-0.275	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.65	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	4.771	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	-2.048	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.361, 0.18, 0.41 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.049	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	0, 0	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

S.aureus (Gram-positive)

4.2 Antimicrobial Activity

Amphibian defense peptide, Antibiotic, Antimicrobial, Antiviral protein, Fungicide, Anti-HSV, Anti-MRSA, Anti-biofilm, Anti-parasitic, Anti-gram-Positive

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Hemolytic, Synergistic peptide, Wound healing, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: Simmaco M, Mignogna G, Canofeni S, et al. Temporins, antimicrobial peptides from the European red frog Rana temporaria. Eur J Biochem. 1996;242(3):788-92. Published 1996 Dec 15. doi:10.1111/j.1432-1033.1996.0788r.x

PMID: 9022710

Citation 2: Samgina TY, Vasileva ID, Kovalev SV, et al. Differentiation of Central Slovenian and Moscow populations of Rana temporaria frogs using peptide biomarkers of temporins family. Anal Bioanal Chem. 2021;413(21):5333-5347. Published 2021 Sep. doi:10.1007/s00216-021-03506-1

PMID: 34235566

Citation 3: Mangoni ML, Rinaldi AC, Di Giulio A, et al. Structure-function relationships of temporins, small antimicrobial peptides from amphibian skin. Eur J Biochem. 2000;267(5):1447-54. Published 2000 Mar. doi:10.1046/j.1432-1327.2000.01143.x

PMID: 10691983

Citation 4: Rinaldi AC, Di Giulio A, Liberi M, et al. Effects of temporins on molecular dynamics and membrane permeabilization in lipid vesicles. J Pept Res. 2001;58(3):213-20. Published 2001 Sep. doi:10.1034/j.1399-3011.2001.00896.x

PMID: 11576327

Citation 5: Mangoni ML, Saugar JM, Dellisanti M, et al. Temporins, small antimicrobial peptides with leishmanicidal activity. J Biol Chem. 2005;280(2):984-90. Published 2005 Jan 14. doi:10.1074/jbc.M410795200

PMID: 15513914

Citation 6: Rosenfeld Y, Barra D, Simmaco M, et al. A synergism between temporins toward Gram-negative bacteria overcomes resistance imposed by the lipopolysaccharide protective layer. J Biol Chem. 2006;281(39):28565-74. Published 2006 Sep 29. doi:10.1074/jbc.M606031200

PMID: 16867990

Citation 7: Di Grazia A, Luca V, Segev-Zarko LA, et al. Temporins A and B stimulate migration of HaCaT keratinocytes and kill intracellular Staphylococcus aureus. Antimicrob Agents Chemother. 2014;58(5):2520-7. Published 2014 May. doi:10.1128/AAC.02801-13

PMID: 24514087

Citation 8: Eggimann GA, Sweeney K, Bolt HL, et al. The role of phosphoglycans in the susceptibility of Leishmania mexicana to the temporin family of anti-microbial peptides. Molecules. 2015;20(2):2775-85. Published 2015 Feb 6. doi:10.3390/molecules20022775

PMID: 25668079

Citation 9: Maisetta G, Grassi L, Di Luca M, et al. Anti-biofilm properties of the antimicrobial peptide temporin 1Tb and its ability, in combination with EDTA, to eradicate Staphylococcus epidermidis biofilms on silicone catheters. Biofouling. 2016;32(7):787-800. Published 2016 Aug. doi:10.1080/08927014.2016.1194401

PMID: 27351824

Citation 10: Grassi L, Maisetta G, Maccari G, et al. Analogs of the Frog-skin Antimicrobial Peptide Temporin 1Tb Exhibit a Wider Spectrum of Activity and a Stronger Antibiofilm Potential as Compared to the Parental Peptide. Front Chem. 2017;5:24. Published 2017. doi:10.3389/fchem.2017.00024

PMID: 28443279

Citation 11: Marcocci ME, Amatore D, Villa S, et al. The Amphibian Antimicrobial Peptide Temporin B Inhibits In Vitro Herpes Simplex Virus 1 Infection. Antimicrob Agents Chemother. 2018;62(5). Published 2018 May. doi:10.1128/AAC.02367-17

PMID: 29483113

Citation 12: Bhunia A, Saravanan R, Mohanram H, et al. NMR structures and interactions of temporin-1Tl and temporin-1Tb with lipopolysaccharide micelles: mechanistic insights into outer membrane permeabilization and synergistic activity. J Biol Chem. 2011;286(27):24394-406. Published 2011 Jul 8. doi:10.1074/jbc.M110.189662

PMID: 21586570

Citation 13: Manzo G, Ferguson PM, Gustilo VB, et al. Minor sequence modifications in temporin B cause drastic changes in antibacterial potency and selectivity by fundamentally altering membrane activity. Sci Rep. 2019;9(1):1385. Published 2019 Feb 4. doi:10.1038/s41598-018-37630-3

PMID: 30718667

5.2 Protein Sequence Databases

5.3 3D Structure Databases

	Sl. no.	PDB ID	Method	Resolution	Access Links	3D View

AlphaFoldDB: P79874

5.4 Nucleotide Sequence Databases

Sl. no.	Accession(s)	Access Link(s)
1.	Y09393	GenBank \|\| EMBL

RefSeq: Not found

5.5 Protein-Protein Interaction Databases

STRING: Not found

IntAct: Not found

BioGRID: Not found

5.6 Ligand Databases

BindingDB: Not found

DrugBank: Not found

ChEMBL: Not found

5.7 Family & Domain Databases

InterPro: IPR004275

PANTHER: Not found

PROSITE: Not found

5.8 Genome Annotation Databases

Ensembl: Not found

5.9 Phylogenomic Databases

GeneTree: Not found

5.10 Enzyme & Pathway Databases

BRENDA: Not found

BioCyc: Not found

5.11 Protein-RNA Interaction Databases

RNAct: Not found

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