AMPDB_772 | Kalata-B1

1 General Description

AMPDB ID: AMPDB_772

Protein Names: Kalata-B1

Protein Family: Cyclotide family; Moebius subfamily

Gene Name: OAK1

Source Organism: Oldenlandia affinis

Protein Length: 124 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

MAKFTVCLLLCLLLAAFVGAFGSELSDSHKTTLVNEIAEKMLQRKILDGVEATLVTDVAEKMFLRKMKAEAKTSETADQVFLKQLQLKGLPVCGETCVGGTCNTPGCTCSWPVCTRNGLPSLAA

FASTA format

Counts of Amino Acids

'A': 12, 'R': 3, 'N': 3, 'D': 4, 'C': 8, 'Q': 4, 'E': 8, 'G': 9, 'H': 1, 'I': 2, 'L': 18, 'K': 10, 'M': 4, 'F': 5, 'P': 4, 'S': 6, 'T': 12, 'W': 1, 'Y': 0, 'V': 10

Frequencies of Amino Acids

'A': 9.68%, 'R': 2.42%, 'N': 2.42%, 'D': 3.23%, 'C': 6.45%, 'Q': 3.23%, 'E': 6.45%, 'G': 7.26%, 'H': 0.81%, 'I': 1.61%, 'L': 14.52%, 'K': 8.06%, 'M': 3.23%, 'F': 4.03%, 'P': 3.23%, 'S': 4.84%, 'T': 9.68%, 'W': 0.81%, 'Y': 0%, 'V': 8.06%

Missing Amino Acid(s)

Most Occurring Amino Acid(s)

Less Occurring Amino Acid(s)

H, W

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	13270.7 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	95.968	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	44.752	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	0.293	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.596	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	7.638	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	0.606	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.29, 0.177, 0.339 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.048	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	5500, 6000	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

E.coli (Gram-negative), S.aureus (Gram-positive)

4.2 Antimicrobial Activity

Antibiotic, Antimicrobial, Plant defense, Anti-gram-negative, Anti-gram-Positive

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Cytolysis, Anti-uterotonic, Hemolytic, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: Jennings C, West J, Waine C, et al. Biosynthesis and insecticidal properties of plant cyclotides: the cyclic knotted proteins from Oldenlandia affinis. Proc Natl Acad Sci U S A. 2001;98(19):10614-9. Published 2001 Sep 11. doi:10.1073/pnas.191366898

PMID: 11535828

Citation 2: Saether O, Craik DJ, Campbell ID, et al. Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1. Biochemistry. 1995;34(13):4147-58. Published 1995 Apr 4. doi:10.1021/bi00013a002

PMID: 7703226

Citation 3: Plan MR, GÃ¶ransson U, Clark RJ, et al. The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides. Chembiochem. 2007;8(9):1001-11. Published 2007 Jun 18. doi:10.1002/cbic.200700097

PMID: 17534989

Citation 4: Tam JP, Lu YA, Yang JL, et al. An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides. Proc Natl Acad Sci U S A. 1999;96(16):8913-8. Published 1999 Aug 3. doi:10.1073/pnas.96.16.8913

PMID: 10430870

Citation 5: Skjeldal L, Gran L, Sletten K, et al. Refined structure and metal binding site of the kalata B1 peptide. Arch Biochem Biophys. 2002;399(2):142-8. Published 2002 Mar 15. doi:10.1006/abbi.2002.2769

PMID: 11888199

Citation 6: Daly NL, Clark RJ, Craik DJ, et al. Disulfide folding pathways of cystine knot proteins. Tying the knot within the circular backbone of the cyclotides. J Biol Chem. 2003;278(8):6314-22. Published 2003 Feb 21. doi:10.1074/jbc.M210492200

PMID: 12482862

Citation 7: Rosengren KJ, Daly NL, Plan MR, et al. Twists, knots, and rings in proteins. Structural definition of the cyclotide framework. J Biol Chem. 2003;278(10):8606-16. Published 2003 Mar 7. doi:10.1074/jbc.M211147200

PMID: 12482868

Citation 8: Barry DG, Daly NL, Clark RJ, et al. Linearization of a naturally occurring circular protein maintains structure but eliminates hemolytic activity. Biochemistry. 2003;42(22):6688-95. Published 2003 Jun 10. doi:10.1021/bi027323n

PMID: 12779323

5.2 Protein Sequence Databases

5.3 3D Structure Databases

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

AlphaFoldDB: P56254

5.4 Nucleotide Sequence Databases

Sl. no.	Accession(s)	Access Link(s)
1.	AF393825	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: IPR005535, IPR012324, IPR036146

PANTHER: Not found

PROSITE: PS51052, PS60009

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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