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Protein

Kalata-B1

Gene

OAK1

Organism
Oldenlandia affinis
Status
Reviewed-Annotation score: Annotation score: 4 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.PROSITE-ProRule annotation2 Publications

GO - Biological processi

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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesRubiaceaeRubioideaeSpermacoceaeHedyotis-Oldenlandia complexOldenlandia

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000000661723 – 88Add BLAST66
PeptideiPRO_000000661889 – 117Kalata-B1Add BLAST29
PropeptideiPRO_0000006619118 – 1247

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki89 ↔ 117Cyclopeptide (Gly-Asn)
Disulfide bondi93 ↔ 107PROSITE-ProRule annotation1 Publication
Disulfide bondi97 ↔ 109PROSITE-ProRule annotation1 Publication
Disulfide bondi102 ↔ 114PROSITE-ProRule annotation1 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.1 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Leaves and stems. Lower in roots.

Structurei

Secondary structure

1124
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi93 – 96Combined sources4
Beta strandi98 – 100Combined sources3
Beta strandi104 – 106Combined sources3
Beta strandi108 – 110Combined sources3
Beta strandi113 – 116Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2MN1NMR-A89-117[»]
4TTMX-ray1.90A89-117[»]
4TTNX-ray1.25A89-117[»]
4TTOX-ray2.30A89-117[»]
ProteinModelPortaliP56254.
SMRiP56254.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56254.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the cyclotide family. Moebius subfamily.PROSITE-ProRule annotation

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

        10         20         30         40         50
MAKFTVCLLL CLLLAAFVGA FGSELSDSHK TTLVNEIAEK MLQRKILDGV
60 70 80 90 100
EATLVTDVAE KMFLRKMKAE AKTSETADQV FLKQLQLKGL PVCGETCVGG
110 120
TCNTPGCTCS WPVCTRNGLP SLAA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF393825 mRNA. Translation: AAL05477.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2MN1NMR-A89-117[»]
4TTMX-ray1.90A89-117[»]
4TTNX-ray1.25A89-117[»]
4TTOX-ray2.30A89-117[»]
ProteinModelPortaliP56254.
SMRiP56254.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP56254.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

The oxidation forms of Trp-111 are subject of controversy and could be the artifactual results of sample handling.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.