ID   KAB7_OLDAF              Reviewed;         111 AA.
AC   P58457;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Kalata-B7;
DE   Flags: Precursor;
GN   Name=OAK3;
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 76-104, AND MASS SPECTROMETRY.
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).
CC   -!- FUNCTION: Probably participates in a plant defense mechanism. Has
CC       hemolytic activity.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- PTM: Kalata-B7 is a cyclic peptide.
CC   -!- MASS SPECTROMETRY: Mass=3071.6; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17534989};
CC   -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00395}.
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DR   EMBL; AF393827; AAL05479.1; -; mRNA.
DR   PDB; 2JWM; NMR; -; A=80-109.
DR   PDB; 2M9O; NMR; -; A=76-104.
DR   PDB; 2MW0; NMR; -; A=76-96.
DR   PDBsum; 2JWM; -.
DR   PDBsum; 2M9O; -.
DR   PDBsum; 2MW0; -.
DR   AlphaFoldDB; P58457; -.
DR   BMRB; P58457; -.
DR   SMR; P58457; -.
DR   EvolutionaryTrace; P58457; -.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR005535; Cyclotide.
DR   InterPro; IPR012324; Cyclotide_moebius_CS.
DR   InterPro; IPR036146; Cyclotide_sf.
DR   Pfam; PF03784; Cyclotide; 1.
DR   SUPFAM; SSF57038; SSF57038; 1.
DR   PROSITE; PS51052; CYCLOTIDE; 1.
DR   PROSITE; PS60009; CYCLOTIDE_MOEBIUS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytolysis; Direct protein sequencing; Disulfide bond;
KW   Hemolysis; Knottin; Plant defense; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..75
FT                   /evidence="ECO:0000269|PubMed:17534989"
FT                   /id="PRO_0000006632"
FT   PEPTIDE         76..104
FT                   /note="Kalata-B7"
FT                   /id="PRO_0000006633"
FT   PROPEP          105..111
FT                   /id="PRO_0000006634"
FT   DISULFID        80..94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        84..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        89..101
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        76..104
FT                   /note="Cyclopeptide (Gly-Asn)"
FT   STRAND          75..78
FT                   /evidence="ECO:0007829|PDB:2MW0"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:2M9O"
FT   STRAND          90..93
FT                   /evidence="ECO:0007829|PDB:2MW0"
FT   STRAND          95..97
FT                   /evidence="ECO:0007829|PDB:2JWM"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:2JWM"
SQ   SEQUENCE   111 AA;  11959 MW;  C0DA8E645B1F8D0B CRC64;
     MAKFTNCLAL CLLLAAVVGA FGVELSEADK SAVVNEIAEK MALQEMLDGV DKLFLRKMKS
     SETTLTMFLK EMQLKGLPVC GETCTLGTCY TQGCTCSWPI CKRNGLPDVA A