ID   ERVB_TABDI              Reviewed;         215 AA.
AC   P60994;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Ervatamin-B;
DE            Short=ERV-B;
DE            EC=3.4.22.-;
OS   Tabernaemontana divaricata (Crepe jasmine) (Ervatamia coronaria).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae;
OC   Tabernaemontaneae; Tabernaemontaninae; Tabernaemontana.
OX   NCBI_TaxID=52861;
RN   [1]
RP   PROTEIN SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX   PubMed=12784208; DOI=10.1002/prot.10319;
RA   Biswas S., Chakrabarti C., Kundu S., Jagannadham M.V., Dattagupta J.K.;
RT   "Proposed amino acid sequence and the 1.63 A X-ray crystal structure of a
RT   plant cysteine protease, ervatamin B: some insights into the structural
RT   basis of its stability and substrate specificity.";
RL   Proteins 51:489-497(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-21, AND CHARACTERIZATION.
RC   TISSUE=Latex;
RX   PubMed=10691612; DOI=10.1021/jf990661j;
RA   Kundu S., Sundd M., Jagannadham M.V.;
RT   "Purification and characterization of a stable cysteine protease ervatamin
RT   B, with two disulfide bridges, from the latex of Ervatamia coronaria.";
RL   J. Agric. Food Chem. 48:171-179(2000).
CC   -!- FUNCTION: Cysteine protease.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Active from pH 3.0 to 10.5.;
CC       Temperature dependence:
CC         Active up to 62 degrees Celsius.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Laticifer.
CC   -!- PTM: Not glycosylated.
CC   -!- MISCELLANEOUS: Stable in 8 M urea and 2.5 M GuHCl at neutral pH, in 40%
CC       acetonitrile, 70% ethanol and 50% methanol. Unstable in SDS.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR   PIR; A59428; A59428.
DR   PDB; 1IWD; X-ray; 1.63 A; A=1-215.
DR   PDBsum; 1IWD; -.
DR   AlphaFoldDB; P60994; -.
DR   SMR; P60994; -.
DR   MEROPS; C01.099; -.
DR   EvolutionaryTrace; P60994; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Protease; Secreted; Thiol protease.
FT   CHAIN           1..215
FT                   /note="Ervatamin-B"
FT                   /id="PRO_0000050558"
FT   ACT_SITE        25
FT   ACT_SITE        158
FT   ACT_SITE        178
FT                   /evidence="ECO:0000250"
FT   DISULFID        22..63
FT   DISULFID        56..96
FT   DISULFID        152..203
FT   HELIX           7..10
FT                   /evidence="ECO:0007829|PDB:1IWD"
FT   STRAND          21..23
FT                   /evidence="ECO:0007829|PDB:1IWD"
FT   HELIX           25..42
FT                   /evidence="ECO:0007829|PDB:1IWD"
FT   HELIX           50..56
FT                   /evidence="ECO:0007829|PDB:1IWD"
FT   HELIX           68..78
FT                   /evidence="ECO:0007829|PDB:1IWD"
FT   TURN            84..86
FT                   /evidence="ECO:0007829|PDB:1IWD"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:1IWD"
FT   HELIX           117..126
FT                   /evidence="ECO:0007829|PDB:1IWD"
FT   STRAND          129..133
FT                   /evidence="ECO:0007829|PDB:1IWD"
FT   HELIX           138..141
FT                   /evidence="ECO:0007829|PDB:1IWD"
FT   STRAND          145..148
FT                   /evidence="ECO:0007829|PDB:1IWD"
FT   STRAND          158..168
FT                   /evidence="ECO:0007829|PDB:1IWD"
FT   STRAND          171..177
FT                   /evidence="ECO:0007829|PDB:1IWD"
FT   STRAND          189..193
FT                   /evidence="ECO:0007829|PDB:1IWD"
FT   HELIX           202..204
FT                   /evidence="ECO:0007829|PDB:1IWD"
FT   STRAND          210..213
FT                   /evidence="ECO:0007829|PDB:1IWD"
SQ   SEQUENCE   215 AA;  23183 MW;  4DE62E43BA4F4F83 CRC64;
     LPSFVDWRSK GAVNSIKNQK QCGSCWAFSA VAAVESINKI RTGQLISLSE QELVDCDTAS
     HGCNGGWMNN AFQYIITNGG IDTQQNYPYS AVQGSCKPYR LRVVSINGFQ RVTRNNESAL
     QSAVASQPVS VTVEAAGAPF QHYSSGIFTG PCGTAQNHGV VIVGYGTQSG KNYWIVRNSW
     GQNWGNQGYI WMERNVASSA GLCGIAQLPS YPTKA