[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1073/pnas.191366898; PubMed=11535828 [NCBI, ExPASy, EBI, Israel, Japan] Jennings C.V., West J., Waine C., Craik D.J., Anderson M.A.; "Biosynthesis and insecticidal properties of plant cyclotides: the cyclic knotted proteins from Oldenlandia affinis."; Proc. Natl. Acad. Sci. U.S.A. 98:10614-10619(2001).
[2]	PROTEIN SEQUENCE OF 89-117, MASS SPECTROMETRY, STRUCTURE BY NMR OF 89-109, AND DISULFIDE BONDS. DOI=10.1021/bi00013a002; PubMed=7703226 [NCBI, ExPASy, EBI, Israel, Japan] Saether O., Craik D.J., Campbell I.D., Sletten K., Juul J., Norman D.G.; "Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1."; Biochemistry 34:4147-4158(1995).
[3]	PROTEIN SEQUENCE OF 89-117, FUNCTION, MASS SPECTROMETRY, AND OXIDATION AT TRP-111. DOI=10.1002/cbic.200700097; PubMed=17534989 [NCBI, ExPASy, EBI, Israel, Japan] Plan M.R.R., Goeransson U., Clark R.J., Daly N.L., Colgrave M.L., Craik D.J.; "The cyclotide fingerprint in Oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides."; ChemBioChem 8:1001-1011(2007).
[4]	SYNTHESIS OF 89-117, AND ANTIBACTERIAL ACTIVITY. DOI=10.1073/pnas.96.16.8913; PubMed=10430870 [NCBI, ExPASy, EBI, Israel, Japan] Tam J.P., Lu Y.-A., Yang J.-L., Chiu K.-W.; "An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides."; Proc. Natl. Acad. Sci. U.S.A. 96:8913-8918(1999).
[5]	STRUCTURE BY NMR OF 89-117. DOI=10.1006/abbi.2002.2769; PubMed=11888199 [NCBI, ExPASy, EBI, Israel, Japan] Skjeldal L., Gran L., Sletten K., Volkman B.F.; "Refined structure and metal binding site of the kalata B1 peptide."; Arch. Biochem. Biophys. 399:142-148(2002).
[6]	STRUCTURE BY NMR OF 89-117. DOI=10.1074/jbc.M210492200; PubMed=12482862 [NCBI, ExPASy, EBI, Israel, Japan] Daly N.L., Clark R.J., Craik D.J.; "Disulfide folding pathways of cystine knot proteins. Tying the knot within the circular backbone of the cyclotides."; J. Biol. Chem. 278:6314-6322(2003).
[7]	STRUCTURE BY NMR OF 89-117. DOI=10.1074/jbc.M211147200; PubMed=12482868 [NCBI, ExPASy, EBI, Israel, Japan] Rosengren K.J., Daly N.L., Plan M.R.R., Waine C., Craik D.J.; "Twists, knots, and rings in proteins. Structural definition of the cyclotide framework."; J. Biol. Chem. 278:8606-8616(2003).
[8]	STRUCTURE BY NMR OF 92-115, AND FUNCTION. DOI=10.1021/bi027323n; PubMed=12779323 [NCBI, ExPASy, EBI, Israel, Japan] Barry D.G., Daly N.L., Clark R.J., Sando L., Craik D.J.; "Linearization of a naturally occurring circular protein maintains structure but eliminates hemolytic activity."; Biochemistry 42:6688-6695(2003).

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 Staphylococcus aureus with a minimum inhibition concentration of approximately 0.2 microM. Relatively ineffective against Gram-negative bacteria such as Escherichia coli and Pseudomonas aeruginosa. Inhibitory effect on the growth and development of larvae from Helicoverpa 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.
PTM: 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.
MASS SPECTROMETRY: Mass=2892; Method=Electrospray; Range=89-117; Source=PubMed:7703226;.
MASS SPECTROMETRY: Mass=2982.4; Method=Electrospray; Range=89-117; Source=PubMed:17534989;.
MASS SPECTROMETRY: Mass=2908.4; Method=Electrospray; Range=89-117; Note=With oxindolylalanine; Source=PubMed:17534989;.
MASS SPECTROMETRY: Mass=2924.4; Method=Electrospray; Range=89-117; Note=With N-formylkynurenine; Source=PubMed:17534989;.
PHARMACEUTICAL: 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.
SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
WEB RESOURCE: Name=Protein Spotlight; Note=The protein with a topological twist - Issue 20 of March 2002; URL="http://www.expasy.org/spotlight/back_issues/sptlt020.shtml";.

Copyright

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Cross-references

Sequence databases

EMBL

AF393825; AAL05477.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1JJZ; NMR; -; A=89-117.	[ExPASy / RCSB / EBI]
1K48; NMR; -; A=89-117.	[ExPASy / RCSB / EBI]
1KAL; NMR; -; A=89-109.	[ExPASy / RCSB / EBI]
1N1U; NMR; -; A=89-117.	[ExPASy / RCSB / EBI]
1NB1; NMR; -; A=89-117.	[ExPASy / RCSB / EBI]
1ORX; NMR; -; A=92-115.	[ExPASy / RCSB / EBI]
2F2I; NMR; -; A=89-117.	[ExPASy / RCSB / EBI]
2F2J; NMR; -; A=89-117.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1JJZ; -.
1K48; -.
1KAL; -.
1N1U; -.
1NB1; -.
1ORX; -.
2F2I; -.
2F2J; -.

ModBase

P56254.

Family and domain databases

InterPro

IPR005535; Cyclotide.
IPR012324; Cyclotide_moebius_CS.
Graphical view of domain structure.

Pfam

PF03784; Cyclotide; 1.
Pfam graphical view of domain structure.

PROSITE

PS51052; CYCLOTIDE; 1.
PS60009; CYCLOTIDE_MOEBIUS; 1.
PROSITE graphical view of domain structure (profiles).

Other

P56254; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Hemolysis; Knottin; Oxidation; Pharmaceutical; Plant defense; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`	`Potential.`
`PROPEP`	`23 88`	`66`		`PRO_0000006617`
`PEPTIDE`	`89 117`	`29`	`Kalata-B1.`	`PRO_0000006618`
`PROPEP`	`118 124`	`7`		`PRO_0000006619`
`SITE`	`111 111`	`1`	`Susceptible to oxidation.`
`DISULFID`	`93 107`
`DISULFID`	`97 109`
`DISULFID`	`102 114`
`CROSSLNK`	`89 117`		`Cyclopeptide (Gly-Asn).`
`STRAND`	`98 100`	`3`
`STRAND`	`111 113`	`3`

Sequence information

Length: 124 AA [This is the length of the unprocessed precursor]

Molecular weight: 13271 Da [This is the MW of the unprocessed precursor]

CRC64: 4EAD1D69318FCCC9 [This is a checksum on the sequence]

        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

P56254 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools