ID   FKBP2_SPIOL             Reviewed;          17 AA.
AC   P83061;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Probable FKBP-type peptidyl-prolyl cis-trans isomerase 2, chloroplastic;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
DE   Flags: Fragment;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Leaf {ECO:0000269|PubMed:11719511};
RX   PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA   Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA   Kieselbach T.;
RT   "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL   J. Biol. Chem. 277:8354-8365(2002).
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|UniProtKB:P45878}.
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         Evidence={ECO:0000250|UniProtKB:P45878};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC       {ECO:0000269|PubMed:11719511}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000255}.
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DR   AlphaFoldDB; P83061; -.
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.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Isomerase; Plastid; Rotamase;
KW   Thylakoid.
FT   CHAIN           1..>17
FT                   /note="Probable FKBP-type peptidyl-prolyl cis-trans
FT                   isomerase 2, chloroplastic"
FT                   /id="PRO_0000311683"
FT   NON_TER         17
FT                   /evidence="ECO:0000303|PubMed:11719511"
SQ   SEQUENCE   17 AA;  1771 MW;  E2013F998EFBF908 CRC64;
     AGLPPEEKPK LCDAACE