P56254 (KAB1_OLDAF) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kalata-B1

Gene names

Name:

OAK1

Organism

Oldenlandia affinis

Taxonomic identifier

60225 [NCBI]

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. 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 an herbal tea to accelerate child birth.
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

Ontologies

Keywords
Biological process	Cytolysis Hemolysis Plant defense
Domain	Knottin Signal
Molecular function	Antibiotic Antimicrobial
PTM	Disulfide bond 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 in other organism 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

1 – 22

22

Potential

Propeptide

23 – 88

66

PRO_0000006617

Peptide

89 – 117

29

Kalata-B1 Ref.2 Ref.3

PRO_0000006618

Propeptide

118 – 124

7

PRO_0000006619

Sites

Site

111

1

Susceptible to oxidation

Amino acid modifications

Disulfide bond

93 ↔ 107

Ref.2

Disulfide bond

97 ↔ 109

Ref.2

Disulfide bond

102 ↔ 114

Ref.2

Cross-link

89 ↔ 117

Cyclopeptide (Gly-Asn)

Secondary structure

1

.

.

.

.

.

124

Helix Strand Turn

Details...

Beta strand

98 – 100

3

Beta strand

111 – 113

3

Sequences

	Sequence		Length	Mass (Da)
	P56254 [UniParc]. Last modified December 5, 2001. Version 3. Checksum: 4EAD1D69318FCCC9	FASTA	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

EMBL
GenBank
DDBJ

AF393825 mRNA. Translation: AAL05477.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JJZ	NMR	-	A	89-116	[»]
1K48	NMR	-	A	89-116	[»]
1KAL	NMR	-	A	89-109	[»]
1N1U	NMR	-	A	94-120	[»]
1NB1	NMR	-	A	93-120	[»]
1ORX	NMR	-	A	92-115	[»]
2F2I	NMR	-	A	93-120	[»]
2F2J	NMR	-	A	93-120	[»]
2JUE	NMR	-	A	93-120	[»]
2KHB	NMR	-	A	89-117	[»]

ProteinModelPortal

P56254.

SMR

P56254. Positions 93-120.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR005535. Cyclotide.
IPR012324. Cyclotide_moebius_CS.
[Graphical view]

Pfam

PF03784. Cyclotide. 1 hit.
[Graphical view]

SUPFAM

SSF57038. Cyclotide. 1 hit.

PROSITE

PS51052. CYCLOTIDE. 1 hit.
PS60009. CYCLOTIDE_MOEBIUS. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	September 21, 2011
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program