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P56254 (KAB1_OLDAF) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kalata-B1
Gene names
Name:OAK1
OrganismOldenlandia affinis
Taxonomic identifier60225 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesRubiaceaeRubioideaeSpermacoceaeOldenlandia

Protein attributes

Sequence length124 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.3 Ref.8

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 a herbal tea to accelerate childbirth.

Sequence similarities

Belongs to the cyclotide family. Moebius subfamily.

Mass spectrometry

Molecular mass is 2892 Da from positions 89 - 117. Determined by ESI. Ref.2

Molecular mass is 2982.4 Da from positions 89 - 117. Determined by ESI. Ref.3

Molecular mass is 2908.4 Da from positions 89 - 117. Determined by ESI. With oxindolylalanine. Ref.3

Molecular mass is 2924.4 Da from positions 89 - 117. Determined by ESI. With N-formylkynurenine. Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 8866
PRO_0000006617
Peptide89 – 11729Kalata-B1 Ref.2 Ref.3
PRO_0000006618
Propeptide118 – 1247
PRO_0000006619

Sites

Site1111Susceptible to oxidation

Amino acid modifications

Disulfide bond93 ↔ 107 Ref.2
Disulfide bond97 ↔ 109 Ref.2
Disulfide bond102 ↔ 114 Ref.2
Cross-link89 ↔ 117Cyclopeptide (Gly-Asn)

Secondary structure

........ 124
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56254 [UniParc].

Last modified December 5, 2001. Version 3.
Checksum: 4EAD1D69318FCCC9

FASTA12413,271
        10         20         30         40         50         60 
MAKFTVCLLL CLLLAAFVGA FGSELSDSHK TTLVNEIAEK MLQRKILDGV EATLVTDVAE 

        70         80         90        100        110        120 
KMFLRKMKAE AKTSETADQV FLKQLQLKGL PVCGETCVGG TCNTPGCTCS WPVCTRNGLP 


SLAA 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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

Protein Spotlight

Bio-Art - Issue 53 of December 2004

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF393825 mRNA. Translation: AAL05477.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JJZNMR-A89-116[»]
1K48NMR-A89-116[»]
1KALNMR-A110-120[»]
1N1UNMR-A94-120[»]
1NB1NMR-A93-120[»]
1ORXNMR-A92-115[»]
2F2INMR-A93-121[»]
2F2JNMR-A93-121[»]
2JUENMR-A94-121[»]
2KHBNMR-A89-117[»]
2MH1NMR-A93-120[»]
ProteinModelPortalP56254.
SMRP56254. Positions 93-120.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

TCDB9.B.48.1.1. the cyclotide (cyclotide) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR005535. Cyclotide.
IPR012324. Cyclotide_moebius_CS.
[Graphical view]
PfamPF03784. Cyclotide. 1 hit.
[Graphical view]
SUPFAMSSF57038. SSF57038. 1 hit.
PROSITEPS51052. CYCLOTIDE. 1 hit.
PS60009. CYCLOTIDE_MOEBIUS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP56254.

Entry information

Entry nameKAB1_OLDAF
AccessionPrimary (citable) accession number: P56254
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 5, 2001
Last modified: July 9, 2014
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references