Reviewed,
UniProtKB/Swiss-Prot P56254 (KAB1_OLDAF)
Last modified
November 4, 2008.
Version 66.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Kalata-B1 | ||
| Gene names |
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| Organism | Oldenlandia affinis | ||
| Taxonomic identifier | 60225 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Gentianales › Rubiaceae › Rubioideae › Spermacoceae › Oldenlandia |
Protein attributes
| Sequence length | 124 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Probably participates in a plant defense mechanism. Has antibiotic activity. Has a diuretic effect. Has a uterotonic effect in humans. Active against the Gram-positive S. aureus with a minimum inhibition concentration of approximately 0.2 microM. Relatively ineffective against Gram-negative bacteria such as E.coli and P.aeruginosa. Inhibitory effect on the growth and development of larvae from H.punctigera. The unmodified form has hemolytic activity, the oxidized form lacks hemolytic activity. If the protein is linearized, hemolytic activity is lost. |
| Tissue specificity | Leaves and stems. Lower in roots. |
| Domain | The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. |
| Post-translational modification | Kalata-B1 is a cyclic peptide which occurs in three forms: with unmodified Trp-111, with Trp-111 oxidized to form oxindolylalanine and with Trp-111 oxidized to form N-formylkynurenine. Oxidation is enhanced by exposure to sunlight. |
| Pharmaceutical use | The uteroactive properties of Kalata have been discovered by African traditional medicine. It is used as an ingredient of an herbal tea to accelerate child birth. |
| Sequence similarities | Belongs to the cyclotide family. Moebius subfamily. |
| Mass spectrometry | Molecular weight is 2892 Da from positions 89 - 117. Determined by ESI. Ref.2 Molecular weight is 2982.4 Da from positions 89 - 117. Determined by ESI. Ref.3 Molecular weight is 2908.4 Da from positions 89 - 117. Determined by ESI. With oxindolylalanine. Ref.3 Molecular weight is 2924.4 Da from positions 89 - 117. Determined by ESI. With N-formylkynurenine. Ref.3 |
Ontologies
Keywords | |
|---|---|
| Biological process | Cytolysis Hemolysis Plant defense |
| Domain | Knottin Signal |
| Molecular function | Antibiotic Antimicrobial |
| PTM | Oxidation |
| Technical term | 3D-structure Direct protein sequencing Pharmaceutical |
Gene Ontology (GO) | |
| Biological process | cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW hemolysis by symbiont of host red blood cellsInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||
Molecule processing | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | Potential | ||||||||||
| Propeptide | 23 – 88 | 66 | PRO_0000006617 | ||||||||||
| Peptide | 89 – 117 | 29 | Kalata-B1 | PRO_0000006618 | |||||||||
| Propeptide | 118 – 124 | 7 | PRO_0000006619 | ||||||||||
Sites | |||||||||||||
| Site | 111 | 1 | Susceptible to oxidation | ||||||||||
Amino acid modifications | |||||||||||||
| Disulfide bond | 93 ↔ 107 | ||||||||||||
| Disulfide bond | 97 ↔ 109 | ||||||||||||
| Disulfide bond | 102 ↔ 114 | ||||||||||||
| Cross-link | 89 ↔ 117 | Cyclopeptide (Gly-Asn) | |||||||||||
Secondary structure | |||||||||||||
Helix Strand Turn | |||||||||||||
| Beta strand | 98 – 100 | 3 | |||||||||||
| Beta strand | 111 – 113 | 3 | |||||||||||
Sequences
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References
| [1] | "Biosynthesis and insecticidal properties of plant cyclotides: the cyclic knotted proteins from Oldenlandia affinis." Jennings C.V., West J., Waine C., Craik D.J., Anderson M.A. Proc. Natl. Acad. Sci. U.S.A. 98:10614-10619(2001) [PubMed: 11535828] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1." Saether O., Craik D.J., Campbell I.D., Sletten K., Juul J., Norman D.G. Biochemistry 34:4147-4158(1995) [PubMed: 7703226] [Abstract] Cited for: PROTEIN SEQUENCE OF 89-117, MASS SPECTROMETRY, STRUCTURE BY NMR OF 89-109, DISULFIDE BONDS. |
| [3] | "The cyclotide fingerprint in Oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides." Plan M.R.R., Goeransson U., Clark R.J., Daly N.L., Colgrave M.L., Craik D.J. ChemBioChem 8:1001-1011(2007) [PubMed: 17534989] [Abstract] Cited for: PROTEIN SEQUENCE OF 89-117, FUNCTION, MASS SPECTROMETRY, OXIDATION AT TRP-111. |
| [4] | "An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides." Tam J.P., Lu Y.-A., Yang J.-L., Chiu K.-W. Proc. Natl. Acad. Sci. U.S.A. 96:8913-8918(1999) [PubMed: 10430870] [Abstract] Cited for: SYNTHESIS OF 89-117, ANTIBACTERIAL ACTIVITY. |
| [5] | "Refined structure and metal binding site of the kalata B1 peptide." Skjeldal L., Gran L., Sletten K., Volkman B.F. Arch. Biochem. Biophys. 399:142-148(2002) [PubMed: 11888199] [Abstract] Cited for: STRUCTURE BY NMR OF 89-117. |
| [6] | "Disulfide folding pathways of cystine knot proteins. Tying the knot within the circular backbone of the cyclotides." Daly N.L., Clark R.J., Craik D.J. J. Biol. Chem. 278:6314-6322(2003) [PubMed: 12482862] [Abstract] Cited for: STRUCTURE BY NMR OF 89-117. |
| [7] | "Twists, knots, and rings in proteins. Structural definition of the cyclotide framework." Rosengren K.J., Daly N.L., Plan M.R.R., Waine C., Craik D.J. J. Biol. Chem. 278:8606-8616(2003) [PubMed: 12482868] [Abstract] Cited for: STRUCTURE BY NMR OF 89-117. |
| [8] | "Linearization of a naturally occurring circular protein maintains structure but eliminates hemolytic activity." Barry D.G., Daly N.L., Clark R.J., Sando L., Craik D.J. Biochemistry 42:6688-6695(2003) [PubMed: 12779323] [Abstract] Cited for: STRUCTURE BY NMR OF 92-115, FUNCTION. |
| + | Additional computationally mapped references. |
Web resources
| Protein Spotlight The protein with a topological twist - Issue 20 of March 2002 |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| AF393825 mRNA. Translation: AAL05477.1. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| InterPro | IPR005535. Cyclotide. IPR012324. Cyclotide_moebius_CS. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Pfam | PF03784. Cyclotide. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PROSITE | PS51052. CYCLOTIDE. 1 hit. PS60009. CYCLOTIDE_MOEBIUS. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Other Resources | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| LinkHub | P56254. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Entry information
| Entry name | KAB1_OLDAF | ||||||||
| Accession | Primary (citable) accession number: P56254 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


