ID   PPIA_STRAQ              Reviewed;         165 AA.
AC   Q06118;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase A;
DE            Short=PPIase A;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin ScCypA;
DE   AltName: Full=Cyclophilin homolog;
DE   AltName: Full=Rotamase A;
GN   Name=ppiA;
OS   Streptomyces anulatus (Streptomyces chrysomallus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1892;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 4-41, AND
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 11523 / DSM 40128 / JCM 4296 / LMG 20459 / NBRC 15393;
RX   PubMed=1474897; DOI=10.1111/j.1365-2958.1992.tb01790.x;
RA   Pahl A., Uehlein M., Bang H., Schlumbohm W., Keller U.;
RT   "Streptomycetes possess peptidyl-prolyl cis-trans isomerases that strongly
RT   resemble cyclophilins from eukaryotic organisms.";
RL   Mol. Microbiol. 6:3551-3558(1992).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
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: Binds cyclosporin A (CsA). CsA mediates some of
CC       its effects via an inhibitory action on PPIase.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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DR   EMBL; Z15137; CAA78840.1; -; Genomic_DNA.
DR   PIR; S28020; S28020.
DR   RefSeq; WP_050359445.1; NZ_CM003601.1.
DR   AlphaFoldDB; Q06118; -.
DR   SMR; Q06118; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Isomerase; Rotamase.
FT   CHAIN           1..165
FT                   /note="Peptidyl-prolyl cis-trans isomerase A"
FT                   /id="PRO_0000064206"
FT   DOMAIN          6..164
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   165 AA;  17716 MW;  2CF1DF725CD6F47D CRC64;
     MTTKVYFDIT IDDAPAGRIT FNLFDDVVPK TAENFRALAT GEKGFGYAGS SFHRVITDFM
     LQGGDFTRGD GTGGKSIYGE KFADENFQLK HDRVGLLSMA NAGKNTNGSQ FFITTVLTPW
     LDGKHVVFGE VADDDSMALV RKIEALGSSS GRTSAKVTIA ESGAL