ID   CYPB_VICFA              Reviewed;         248 AA.
AC   Q41651;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase, chloroplastic;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin;
DE   AltName: Full=Cyclosporin A-binding protein;
DE            Short=CYP B;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
OS   Vicia faba (Broad bean) (Faba vulgaris).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX   NCBI_TaxID=3906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   TISSUE=Leaf;
RX   PubMed=8061522; DOI=10.2307/3869966;
RA   Luan S., Lane W.S., Schreiber S.L.;
RT   "pCyP B: a chloroplast-localized, heat shock-responsive cyclophilin from
RT   fava bean.";
RL   Plant Cell 6:885-892(1994).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC       its effects via an inhibitory action on PPIase.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC   -!- TISSUE SPECIFICITY: Highly expressed in leaf.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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DR   EMBL; L32095; AAA64430.1; -; mRNA.
DR   PIR; T12096; T12096.
DR   AlphaFoldDB; Q41651; -.
DR   SMR; Q41651; -.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Isomerase; Plastid; Rotamase;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..248
FT                   /note="Peptidyl-prolyl cis-trans isomerase, chloroplastic"
FT                   /id="PRO_0000025477"
FT   DOMAIN          85..243
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          223..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   248 AA;  26547 MW;  B9688620D40AC257 CRC64;
     MASSFSTQLV QSQNLLPRFH AVQGKPHVVS SIGCSKLSST YHYAPRLSVS QQSKAKSITS
     RRITCASGAQ GEVAELQAKV TSKIFFDIEI GGESAGRIVI GLFGDAVPKT VENFKTLSTG
     AKGYGYQGSF FHRIIPNFMI QGGDFTEGNG TGGVSIYGSK FEDESFDLKH VGPGVLSMAN
     AGPNTNGSQF FICTVPTPWL DNRHVVFGHV IEGLDVVKQL ESQETSKLDN SPKKPCKIAK
     SGELPLDG