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P56254

- KAB1_OLDAF

UniProt

P56254 - KAB1_OLDAF

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Protein
Kalata-B1
Gene
OAK1
Organism
Oldenlandia affinis
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei111 – 1111Susceptible to oxidation

GO - Biological processi

  1. defense response to bacterium Source: UniProtKB-KW
  2. hemolysis in other organism Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial

Keywords - Biological processi

Cytolysis, Hemolysis, Plant defense

Protein family/group databases

TCDBi9.B.48.1.1. the cyclotide (cyclotide) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Kalata-B1
Gene namesi
Name:OAK1
OrganismiOldenlandia affinis
Taxonomic identifieri60225 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesRubiaceaeRubioideaeSpermacoceaeOldenlandia

Pathology & Biotechi

Pharmaceutical usei

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 Reviewed prediction
Add
BLAST
Propeptidei23 – 8866
PRO_0000006617Add
BLAST
Peptidei89 – 11729Kalata-B12 Publications
PRO_0000006618Add
BLAST
Propeptidei118 – 1247
PRO_0000006619

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki89 ↔ 117Cyclopeptide (Gly-Asn)
Disulfide bondi93 ↔ 1071 Publication
Disulfide bondi97 ↔ 1091 Publication
Disulfide bondi102 ↔ 1141 Publication

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, Oxidation

Expressioni

Tissue specificityi

Leaves and stems. Lower in roots.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi98 – 1003
Beta strandi104 – 1063
Beta strandi108 – 1103
Beta strandi111 – 1133

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP56254.
SMRiP56254. Positions 93-120.

Miscellaneous databases

EvolutionaryTraceiP56254.

Family & Domainsi

Domaini

The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.

Sequence similaritiesi

Keywords - Domaini

Knottin, Signal

Family and domain databases

InterProiIPR005535. Cyclotide.
IPR012324. Cyclotide_moebius_CS.
[Graphical view]
PfamiPF03784. Cyclotide. 1 hit.
[Graphical view]
SUPFAMiSSF57038. SSF57038. 1 hit.
PROSITEiPS51052. CYCLOTIDE. 1 hit.
PS60009. CYCLOTIDE_MOEBIUS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P56254-1 [UniParc]FASTAAdd to Basket

« Hide

MAKFTVCLLL CLLLAAFVGA FGSELSDSHK TTLVNEIAEK MLQRKILDGV    50
EATLVTDVAE KMFLRKMKAE AKTSETADQV FLKQLQLKGL PVCGETCVGG 100
TCNTPGCTCS WPVCTRNGLP SLAA 124
Length:124
Mass (Da):13,271
Last modified:December 5, 2001 - v3
Checksum:i4EAD1D69318FCCC9
GO

Mass spectrometryi

Molecular mass is 2892 Da from positions 89 - 117. Determined by ESI. 1 Publication
Molecular mass is 2982.4 Da from positions 89 - 117. Determined by ESI. 1 Publication
Molecular mass is 2908.4 Da from positions 89 - 117. Determined by ESI. With oxindolylalanine.1 Publication
Molecular mass is 2924.4 Da from positions 89 - 117. Determined by ESI. With N-formylkynurenine.1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF393825 mRNA. Translation: AAL05477.1.

Cross-referencesi

Web resourcesi

Protein Spotlight

The protein with a topological twist - Issue 20 of March 2002

Protein Spotlight

Bio-Art - Issue 53 of December 2004

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF393825 mRNA. Translation: AAL05477.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JJZ NMR - A 89-116 [» ]
1K48 NMR - A 89-116 [» ]
1KAL NMR - A 110-120 [» ]
1N1U NMR - A 94-120 [» ]
1NB1 NMR - A 93-120 [» ]
1ORX NMR - A 92-115 [» ]
2F2I NMR - A 93-121 [» ]
2F2J NMR - A 93-121 [» ]
2JUE NMR - A 94-121 [» ]
2KHB NMR - A 89-117 [» ]
2MH1 NMR - A 93-120 [» ]
ProteinModelPortali P56254.
SMRi P56254. Positions 93-120.
ModBasei Search...

Protein family/group databases

TCDBi 9.B.48.1.1. the cyclotide (cyclotide) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P56254.

Family and domain databases

InterProi IPR005535. Cyclotide.
IPR012324. Cyclotide_moebius_CS.
[Graphical view ]
Pfami PF03784. Cyclotide. 1 hit.
[Graphical view ]
SUPFAMi SSF57038. SSF57038. 1 hit.
PROSITEi PS51052. CYCLOTIDE. 1 hit.
PS60009. CYCLOTIDE_MOEBIUS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiKAB1_OLDAF
AccessioniPrimary (citable) accession number: P56254
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Pharmaceutical

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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