ID   KAB3_OLDAF              Reviewed;         158 AA.
AC   P58455;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Kalata-B3/B6;
DE   Contains:
DE     RecName: Full=Kalata-B6;
DE   Contains:
DE     RecName: Full=Kalata-B3;
DE   Flags: Precursor;
GN   Name=OAK2;
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 67-96 AND 122-151, 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).
RN   [3]
RP   STRUCTURE BY NMR OF 48-69.
RX   PubMed=15328347; DOI=10.1074/jbc.m407421200;
RA   Dutton J.L., Renda R.F., Waine C., Clark R.J., Daly N.L., Jennings C.V.,
RA   Anderson M.A., Craik D.J.;
RT   "Conserved structural and sequence elements implicated in the processing of
RT   gene-encoded circular proteins.";
RL   J. Biol. Chem. 279:46858-46867(2004).
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-B3 and kalata-B6 are cyclic peptides.
CC   -!- MASS SPECTROMETRY: [Kalata-B6]: Mass=3029.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17534989};
CC   -!- MASS SPECTROMETRY: [Kalata-B3]: Mass=3082.5; 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; AF393826; AAL05478.1; -; mRNA.
DR   PDB; 1WN8; NMR; -; A=103-124.
DR   PDBsum; 1WN8; -.
DR   AlphaFoldDB; P58455; -.
DR   SMR; P58455; -.
DR   EvolutionaryTrace; P58455; -.
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; 2.
DR   SUPFAM; SSF57038; SSF57038; 2.
DR   PROSITE; PS51052; CYCLOTIDE; 2.
DR   PROSITE; PS60009; CYCLOTIDE_MOEBIUS; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Cytolysis; Direct protein sequencing; Disulfide bond;
KW   Hemolysis; Knottin; Plant defense; Repeat; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..66
FT                   /evidence="ECO:0000269|PubMed:17534989"
FT                   /id="PRO_0000006627"
FT   PEPTIDE         67..96
FT                   /note="Kalata-B6"
FT                   /id="PRO_0000006628"
FT   PROPEP          97..121
FT                   /evidence="ECO:0000269|PubMed:17534989"
FT                   /id="PRO_0000006629"
FT   PEPTIDE         122..151
FT                   /note="Kalata-B3"
FT                   /id="PRO_0000006630"
FT   PROPEP          152..158
FT                   /id="PRO_0000006631"
FT   DISULFID        71..85
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        75..87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        80..93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        126..140
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        130..142
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   DISULFID        135..148
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00395"
FT   CROSSLNK        67..96
FT                   /note="Cyclopeptide (Gly-Asn)"
FT   CROSSLNK        122..151
FT                   /note="Cyclopeptide (Gly-Asp)"
FT   TURN            106..108
FT                   /evidence="ECO:0007829|PDB:1WN8"
FT   HELIX           109..120
FT                   /evidence="ECO:0007829|PDB:1WN8"
SQ   SEQUENCE   158 AA;  16643 MW;  A5C3B4DAB8503F3B CRC64;
     MAKFTKSLVL CLLLAAFVGA FGAELSEADK ANVVNEIAAN IQREILKGVK SSETTLTMFL
     KEMQLKGLPT CGETCFGGTC NTPGCSCSSW PICTRNGLPK RAGVKSSETT LTMFLKEMQL
     KGLPTCGETC FGGTCNTPGC TCDPWPICTR DGLPSAAA