ID   TLP20_SPIOL             Reviewed;          45 AA.
AC   P82536;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 2.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase TLP20, chloroplastic;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=P18;
DE   AltName: Full=Rotamase;
DE   AltName: Full=Thylakoid lumen PPIase of 20 kDa;
DE   AltName: Full=Thylakoid lumenal 18 kDa protein;
DE   Flags: Fragments;
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]
RP   PROTEIN SEQUENCE OF 1-20, AND SUBCELLULAR LOCATION.
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).
RN   [2]
RP   SEQUENCE REVISION TO 16.
RA   Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA   Kieselbach T.;
RL   Submitted (JUN-2003) to UniProtKB.
RN   [3]
RP   PROTEIN SEQUENCE OF 1-10 AND 15-45, FUNCTION, AND REGULATION.
RX   PubMed=12729913; DOI=10.1016/s0014-5793(03)00366-1;
RA   Edvardsson A., Eshaghi S., Vener A.V., Andersson B.;
RT   "The major peptidyl-prolyl isomerase activity in thylakoid lumen of plant
RT   chloroplasts belongs to a novel cyclophilin TLP20.";
RL   FEBS Lett. 542:137-141(2003).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. {ECO:0000269|PubMed:12729913}.
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:11719511}.
CC   -!- MISCELLANEOUS: Was originally reported as TL18.
CC       {ECO:0000305|PubMed:11719511}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P82536; -.
DR   SMR; P82536; -.
DR   IntAct; P82536; 1.
DR   BRENDA; 5.2.1.8; 5812.
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   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   SUPFAM; SSF50891; SSF50891; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Isomerase; Plastid; Rotamase;
KW   Thylakoid.
FT   CHAIN           1..>45
FT                   /note="Peptidyl-prolyl cis-trans isomerase TLP20,
FT                   chloroplastic"
FT                   /id="PRO_0000064216"
FT   DOMAIN          11..>45
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   NON_CONS        27..28
FT                   /evidence="ECO:0000305"
FT   NON_TER         45
SQ   SEQUENCE   45 AA;  4881 MW;  36155223724C01EA CRC64;
     SAEETPLQSK VTNKVYFDIS IGNPVGKVVI GLFGDDVPQT AENFR