ID   FKBP3_VICFA             Reviewed;          45 AA.
AC   P59724;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase, chloroplastic;
DE            EC=5.2.1.8;
DE   AltName: Full=PPIase;
DE   AltName: Full=Rotamase;
DE   AltName: Full=VfFKBP13;
DE   Flags: Fragment;
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   PROTEIN SEQUENCE.
RX   PubMed=12424338; DOI=10.1073/pnas.222550399;
RA   Gupta R., Mould R.M., He Z., Luan S.;
RT   "A chloroplast FKBP interacts with and affects the accumulation of Rieske
RT   subunit of cytochrome bf complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:15806-15811(2002).
RN   [2]
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=7508125; DOI=10.1073/pnas.91.3.984;
RA   Luan S., Albers M.W., Schreiber S.L.;
RT   "Light-regulated, tissue-specific immunophilins in a higher plant.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:984-988(1994).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC       {ECO:0000269|PubMed:7508125}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, but not in roots.
CC       {ECO:0000269|PubMed:7508125}.
CC   -!- DEVELOPMENTAL STAGE: Not expressed in etiolated leaves.
CC       {ECO:0000269|PubMed:7508125}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   AlphaFoldDB; P59724; -.
DR   SMR; P59724; -.
DR   GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR044609; FKBP2/11.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   PANTHER; PTHR45779; PTHR45779; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Isomerase; Plastid; Rotamase;
KW   Thylakoid.
FT   CHAIN           1..>45
FT                   /note="FKBP-type peptidyl-prolyl cis-trans isomerase,
FT                   chloroplastic"
FT                   /id="PRO_0000075349"
FT   NON_TER         45
SQ   SEQUENCE   45 AA;  4625 MW;  3F9094DFBC8DA017 CRC64;
     AAEVAPCELT VAPSGLSFCD KVVGTGPQAV KGQLIKAHYV GRLEN