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   16-JUN-2009, entry version 55.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase, chloroplastic;
DE            Short=PPIase;
DE            Short=Rotamase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin;
DE   AltName: Full=Cyclosporin A-binding protein;
DE            Short=CYP B;
DE   Flags: Precursor;
OS   Vicia faba (Broad bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Fabeae; Vicia.
OX   NCBI_TaxID=3906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP   CHARACTERIZATION.
RC   TISSUE=Leaf;
RX   MEDLINE=94339699; PubMed=8061522; DOI=10.1105/tpc.6.6.885;
RA   Luan S., Lane W.S., Schreiber S.L.;
RT   "pCyP B: a chloroplast-localized, heat shock-responsive cyclophilin
RT   from fava bean.";
RL   Plant Cell 6:885-892(1994).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- ENZYME 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   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
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DR   EMBL; L32095; AAA64430.1; -; mRNA.
DR   PIR; T12096; T12096.
DR   HSSP; P52011; 1E3B.
DR   BRENDA; 5.2.1.8; 30.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0042277; F:peptide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   InterPro; IPR002130; PPIase_cyclophilin.
DR   Gene3D; G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Cyclosporin; Direct protein sequencing; Isomerase;
KW   Plastid; Rotamase; Transit peptide.
FT   TRANSIT       1      ?       Chloroplast (Potential).
FT   CHAIN         ?    248       Peptidyl-prolyl cis-trans isomerase,
FT                                chloroplastic.
FT                                /FTId=PRO_0000025477.
FT   DOMAIN       85    243       PPIase cyclophilin-type.
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
//