ID   TLP40_SPIOL             Reviewed;         449 AA.
AC   O49939;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase, chloroplastic;
DE            EC=5.2.1.8;
DE   AltName: Full=40 kDa thylakoid lumen PPIase;
DE   AltName: Full=40 kDa thylakoid lumen rotamase;
DE   Flags: Precursor;
GN   Name=TLP40; Synonyms=TLR40;
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   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   STRAIN=cv. Monatol; TISSUE=Green leaf;
RX   PubMed=9501079; DOI=10.1093/emboj/17.6.1577;
RA   Fulgosi H., Vener A.V., Altschmied L., Herrmann R.G., Andersson B.;
RT   "A novel multi-functional chloroplast protein: identification of a 40 kDa
RT   immunophilin-like protein located in the thylakoid lumen.";
RL   EMBO J. 17:1577-1587(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 105-134.
RC   TISSUE=Leaf;
RX   PubMed=9506969; DOI=10.1074/jbc.273.12.6710;
RA   Kieselbach T., Hagman A., Andersson B., Schroeder W.P.;
RT   "The thylakoid lumen of chloroplasts. Isolation and characterization.";
RL   J. Biol. Chem. 273:6710-6716(1998).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. Has a regulatory effect on thylakoid protein
CC       phosphorylation.
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: Does not bind cyclosporin A (CsA).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. Note=Can
CC       interact with the inner surface of the stroma-exposed thylakoid
CC       regions.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y12071; CAA72792.1; -; mRNA.
DR   PIR; T09212; T09212.
DR   AlphaFoldDB; O49939; -.
DR   SMR; O49939; -.
DR   PRIDE; O49939; -.
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:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 1.20.120.290; -; 1.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044665; E_coli_cyclophilin_A-like.
DR   InterPro; IPR023222; PsbQ-like_dom_sf.
DR   PANTHER; PTHR43246; PTHR43246; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   SUPFAM; SSF101112; SSF101112; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Isomerase; Plastid; Rotamase;
KW   Thylakoid; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   TRANSIT         ?..104
FT                   /note="Thylakoid"
FT                   /evidence="ECO:0000269|PubMed:9506969"
FT   CHAIN           105..449
FT                   /note="Peptidyl-prolyl cis-trans isomerase, chloroplastic"
FT                   /id="PRO_0000025505"
FT   DOMAIN          257..449
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   449 AA;  49872 MW;  C8A40195128F15B1 CRC64;
     MSSFINHHFY PSVCTSKHAL PINPTSPFYL GIPNFRQKSR FMHLTPRCFS RQIDPLDKQK
     KRSFSVKECA ISLALAAALI SGVPSLSWER HAEALTSPVL PDLAVLISGP PIKDPEALLR
     YALPIDNKAI REVQKPLEDI TESLRVLGLK ALDSVERNLK QASRALKNGK SLIIAGLAES
     KKDRGVELLD KLEAGMGELQ QIVENRNREG VAPKQRELLQ YVGSVEEDMV DGFPYEVPEE
     YQTMPLLKGR AVVEMKVKVK DNPNVDNCVF RIVLDGYNAP VTAGNFLDLV ERHFYDGMEI
     QRRDGFVVQT GDPEGPAEGF IDPSTEKPRT IPLEIMVEGE KVPVYGSTLE ELGLYKAQTK
     LPFNAFGTMA MAREEFENNS GSSQIFWLLK ESELTPSNAN ILDGRYAVFG YVTDNQDYLA
     DLKVGDVIES VQAVSGVDNL VNPTYKIAG