ID   KAB1_OLDAF              Reviewed;         124 AA.
AC   P56254;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 3.
DT   03-MAY-2023, entry version 113.
DE   RecName: Full=Kalata-B1;
DE   Flags: Precursor;
GN   Name=OAK1;
OS   Oldenlandia affinis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Rubiaceae; Rubioideae; Spermacoceae;
OC   Hedyotis-Oldenlandia complex; Oldenlandia.
OX   NCBI_TaxID=60225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11535828; DOI=10.1073/pnas.191366898;
RA   Jennings C.V., West J., Waine C., Craik D.J., Anderson M.A.;
RT   "Biosynthesis and insecticidal properties of plant cyclotides: the cyclic
RT   knotted proteins from Oldenlandia affinis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:10614-10619(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 89-117, MASS SPECTROMETRY, STRUCTURE BY NMR OF 89-109,
RP   AND DISULFIDE BONDS.
RX   PubMed=7703226; DOI=10.1021/bi00013a002;
RA   Saether O., Craik D.J., Campbell I.D., Sletten K., Juul J., Norman D.G.;
RT   "Elucidation of the primary and three-dimensional structure of the
RT   uterotonic polypeptide kalata B1.";
RL   Biochemistry 34:4147-4158(1995).
RN   [3]
RP   PROTEIN SEQUENCE OF 89-117, FUNCTION, MASS SPECTROMETRY, AND OXIDATION.
RX   PubMed=17534989; DOI=10.1002/cbic.200700097;
RA   Plan M.R.R., Goeransson U., Clark R.J., Daly N.L., Colgrave M.L.,
RA   Craik D.J.;
RT   "The cyclotide fingerprint in Oldenlandia affinis: elucidation of
RT   chemically modified, linear and novel macrocyclic peptides.";
RL   ChemBioChem 8:1001-1011(2007).
RN   [4]
RP   SYNTHESIS OF 89-117, AND ANTIBACTERIAL ACTIVITY.
RX   PubMed=10430870; DOI=10.1073/pnas.96.16.8913;
RA   Tam J.P., Lu Y.-A., Yang J.-L., Chiu K.-W.;
RT   "An unusual structural motif of antimicrobial peptides containing end-to-
RT   end macrocycle and cystine-knot disulfides.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:8913-8918(1999).
RN   [5]
RP   STRUCTURE BY NMR OF 89-117.
RX   PubMed=11888199; DOI=10.1006/abbi.2002.2769;
RA   Skjeldal L., Gran L., Sletten K., Volkman B.F.;
RT   "Refined structure and metal binding site of the kalata B1 peptide.";
RL   Arch. Biochem. Biophys. 399:142-148(2002).
RN   [6]
RP   STRUCTURE BY NMR OF 89-117.
RX   PubMed=12482862; DOI=10.1074/jbc.m210492200;
RA   Daly N.L., Clark R.J., Craik D.J.;
RT   "Disulfide folding pathways of cystine knot proteins. Tying the knot within
RT   the circular backbone of the cyclotides.";
RL   J. Biol. Chem. 278:6314-6322(2003).
RN   [7]
RP   STRUCTURE BY NMR OF 89-117.
RX   PubMed=12482868; DOI=10.1074/jbc.m211147200;
RA   Rosengren K.J., Daly N.L., Plan M.R.R., Waine C., Craik D.J.;
RT   "Twists, knots, and rings in proteins. Structural definition of the
RT   cyclotide framework.";
RL   J. Biol. Chem. 278:8606-8616(2003).
RN   [8]
RP   STRUCTURE BY NMR OF 92-115, AND FUNCTION.
RX   PubMed=12779323; DOI=10.1021/bi027323n;
RA   Barry D.G., Daly N.L., Clark R.J., Sando L., Craik D.J.;
RT   "Linearization of a naturally occurring circular protein maintains
RT   structure but eliminates hemolytic activity.";
RL   Biochemistry 42:6688-6695(2003).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism. Has
CC       antibiotic activity. Has a diuretic effect. Has a uterotonic effect in
CC       humans. Active against the Gram-positive S.aureus with a minimum
CC       inhibition concentration of approximately 0.2 microM. Relatively
CC       ineffective against Gram-negative bacteria such as E.coli and
CC       P.aeruginosa. Inhibitory effect on the growth and development of larvae
CC       from H.punctigera. The unmodified form has hemolytic activity, the
CC       oxidized form lacks hemolytic activity. If the protein is linearized,
CC       hemolytic activity is lost. {ECO:0000255|PROSITE-ProRule:PRU00395,
CC       ECO:0000269|PubMed:12779323, ECO:0000269|PubMed:17534989}.
CC   -!- TISSUE SPECIFICITY: Leaves and stems. Lower in roots.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC   -!- PTM: Kalata-B1 is a cyclic peptide which occurs in three forms: with
CC       unmodified Trp-111, with Trp-111 oxidized to form oxindolylalanine and
CC       with Trp-111 oxidized to form N-formylkynurenine. Oxidation is enhanced
CC       by exposure to sunlight. {ECO:0000269|PubMed:17534989}.
CC   -!- MASS SPECTROMETRY: Mass=2892; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:7703226};
CC   -!- MASS SPECTROMETRY: Mass=2982.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17534989};
CC   -!- MASS SPECTROMETRY: Mass=2908.4; Method=Electrospray; Note=With
CC       oxindolylalanine.; Evidence={ECO:0000269|PubMed:17534989};
CC   -!- MASS SPECTROMETRY: Mass=2924.4; Method=Electrospray; Note=With N-
CC       formylkynurenine.; Evidence={ECO:0000269|PubMed:17534989};
CC   -!- PHARMACEUTICAL: The uteroactive properties of Kalata have been
CC       discovered by African traditional medicine. It is used as an ingredient
CC       of a herbal tea to accelerate childbirth.
CC   -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
CC   -!- CAUTION: The oxidation forms of Trp-111 are subject of controversy and
CC       could be the artifactual results of sample handling.
CC       {ECO:0000305|PubMed:17534989}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=The protein with a
CC       topological twist - Issue 20 of March 2002;
CC       URL="https://web.expasy.org/spotlight/back_issues/020";
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Bio-Art - Issue 53 of
CC       December 2004;
CC       URL="https://web.expasy.org/spotlight/back_issues/053/";
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DR   EMBL; AF393825; AAL05477.1; -; mRNA.
DR   PDB; 1JJZ; NMR; -; A=89-116.
DR   PDB; 1K48; NMR; -; A=89-116.
DR   PDB; 1KAL; NMR; -; A=110-120.
DR   PDB; 1N1U; NMR; -; A=94-120.
DR   PDB; 1NB1; NMR; -; A=93-120.
DR   PDB; 1ORX; NMR; -; A=92-115.
DR   PDB; 2F2I; NMR; -; A=93-121.
DR   PDB; 2F2J; NMR; -; A=93-121.
DR   PDB; 2JUE; NMR; -; A=94-121.
DR   PDB; 2KHB; NMR; -; A=89-117.
DR   PDB; 2MH1; NMR; -; A=93-120.
DR   PDB; 2MN1; NMR; -; A=89-117.
DR   PDB; 4TTM; X-ray; 1.90 A; A=89-117.
DR   PDB; 4TTN; X-ray; 1.25 A; A=89-117.
DR   PDB; 4TTO; X-ray; 2.30 A; A=89-117.
DR   PDB; 7LHC; NMR; -; A=89-117.
DR   PDBsum; 1JJZ; -.
DR   PDBsum; 1K48; -.
DR   PDBsum; 1KAL; -.
DR   PDBsum; 1N1U; -.
DR   PDBsum; 1NB1; -.
DR   PDBsum; 1ORX; -.
DR   PDBsum; 2F2I; -.
DR   PDBsum; 2F2J; -.
DR   PDBsum; 2JUE; -.
DR   PDBsum; 2KHB; -.
DR   PDBsum; 2MH1; -.
DR   PDBsum; 2MN1; -.
DR   PDBsum; 4TTM; -.
DR   PDBsum; 4TTN; -.
DR   PDBsum; 4TTO; -.
DR   PDBsum; 7LHC; -.
DR   AlphaFoldDB; P56254; -.
DR   BMRB; P56254; -.
DR   SMR; P56254; -.
DR   TCDB; 1.A.118.1.1; the plant cycltide (cyclotide) family.
DR   EvolutionaryTrace; P56254; -.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   DisProt; DP01017; -.
DR   InterPro; IPR005535; Cyclotide.
DR   InterPro; IPR012324; Cyclotide_moebius_CS.
DR   InterPro; IPR036146; Cyclotide_sf.
DR   Pfam; PF03784; Cyclotide; 1.
DR   SUPFAM; SSF57038; Cyclotides; 1.
DR   PROSITE; PS51052; CYCLOTIDE; 1.
DR   PROSITE; PS60009; CYCLOTIDE_MOEBIUS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Disulfide bond; Hemolysis; Knottin;
KW   Pharmaceutical; Plant defense; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..88
FT                   /id="PRO_0000006617"
FT   PEPTIDE         89..117
FT                   /note="Kalata-B1"
FT                   /id="PRO_0000006618"
FT   PROPEP          118..124
FT                   /id="PRO_0000006619"
FT   DISULFID        93..107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:7703226"
FT   DISULFID        97..109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:7703226"
FT   DISULFID        102..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395,
FT                   ECO:0000269|PubMed:7703226"
FT   CROSSLNK        89..117
FT                   /note="Cyclopeptide (Gly-Asn)"
FT   STRAND          93..96
FT                   /evidence="ECO:0007829|PDB:4TTN"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:1JJZ"
FT   STRAND          104..106
FT                   /evidence="ECO:0007829|PDB:1K48"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:4TTN"
FT   STRAND          113..116
FT                   /evidence="ECO:0007829|PDB:4TTN"
SQ   SEQUENCE   124 AA;  13271 MW;  4EAD1D69318FCCC9 CRC64;
     MAKFTVCLLL CLLLAAFVGA FGSELSDSHK TTLVNEIAEK MLQRKILDGV EATLVTDVAE
     KMFLRKMKAE AKTSETADQV FLKQLQLKGL PVCGETCVGG TCNTPGCTCS WPVCTRNGLP
     SLAA
//