Kalata-B1 precursor - Oldenlandia affinis

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Reviewed, UniProtKB/Swiss-Prot P56254 (KAB1_OLDAF)

Last modified November 4, 2008. Version 66. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
Kalata-B1

Gene names

Name:

OAK1

Organism

Oldenlandia affinis

Taxonomic identifier

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 bacterium Inferred from electronic annotation. Source: UniProtKB-KW hemolysis by symbiont of host red blood cells Inferred 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

22

Potential

Propeptide

66

PRO_0000006617

Peptide

29

Kalata-B1

PRO_0000006618

Propeptide

7

PRO_0000006619

Sites

Site

1

Susceptible to oxidation

Amino acid modifications

Disulfide bond

Disulfide bond

Disulfide bond

Cross-link

Cyclopeptide (Gly-Asn)

Secondary structure

1

.

.

.

.

.

124

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P56254-1 [UniParc].

Last modified December 5, 2001. Version 3.
Checksum: 4EAD1D69318FCCC9
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124

13,271

        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

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

AF393825 mRNA. Translation: AAL05477.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JJZ	NMR	-	A	89-117	[»]
1K48	NMR	-	A	89-117	[»]
1KAL	NMR	-	A	89-109	[»]
1N1U	NMR	-	A	89-117	[»]
1NB1	NMR	-	A	89-117	[»]
1ORX	NMR	-	A	92-115	[»]
2F2I	NMR	-	A	89-117	[»]
2F2J	NMR	-	A	89-117	[»]

ModBase

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

Other Resources

LinkHub

Entry information

Entry name

KAB1_OLDAF

Accession

Primary (citable) accession number: P56254

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	December 5, 2001
Last modified:	November 4, 2008
This is version 66 of the entry and version 3 of the sequence. [Complete history]

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents