ID   PPIB_STRAT              Reviewed;         166 AA.
AC   P83221; Q6VBU8;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase cyp18;
DE            Short=PPIase cyp18;
DE            Short=SanCyp18;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase cyp18;
GN   Name=cyp18 {ECO:0000312|EMBL:AAQ88274.1};
OS   Streptomyces antibioticus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1890;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 11891 / DSM 40868 / BCRC 11580 / NCIMB 11506 / PSA 205;
RX   PubMed=15304318; DOI=10.1016/j.febslet.2004.06.091;
RA   Manteca A., Kamphausen T., Fanghanel J., Fischer G., Sanchez J.;
RT   "Cloning and characterization of a Streptomyces antibioticus ATCC11891
RT   cyclophilin related to Gram negative bacteria cyclophilins.";
RL   FEBS Lett. 572:19-26(2004).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-21, AND PRELIMINARY CHARACTERIZATION.
RC   STRAIN=ATCC 11891 / DSM 40868 / BCRC 11580 / NCIMB 11506 / PSA 205;
RX   PubMed=10400660; DOI=10.1074/jbc.274.29.20366;
RA   Nicieza R.G., Huergo J., Connolly B.A., Sanchez J.;
RT   "Purification, characterization, and role of nucleases and serine proteases
RT   in Streptomyces differentiation. Analogies with the biochemical processes
RT   described in late steps of eukaryotic apoptosis.";
RL   J. Biol. Chem. 274:20366-20375(1999).
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:10400660}.
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:0000269|PubMed:10400660};
CC   -!- ACTIVITY REGULATION: Inhibition by cyclosporin A with a Ki of 21 mu-
CC       mol.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8-8.5.;
CC   -!- SUBUNIT: Monomer. {ECO:0000303|PubMed:10400660, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15304318}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000255|RuleBase:RU000493}.
CC   -!- CAUTION: Was originally thought to have an endonuclease activity.
CC       {ECO:0000305|PubMed:10400660}.
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; AY343890; AAQ88274.1; -; Genomic_DNA.
DR   AlphaFoldDB; P83221; -.
DR   SMR; P83221; -.
DR   MINT; P83221; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR   GO; GO:0004519; F:endonuclease activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; TAS:UniProtKB.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006308; P:DNA catabolic process; IDA:UniProtKB.
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   InterPro; IPR044665; E_coli_cyclophilin_A-like.
DR   PANTHER; PTHR43246; PTHR43246; 1.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10400660"
FT   CHAIN           2..166
FT                   /note="Peptidyl-prolyl cis-trans isomerase cyp18"
FT                   /id="PRO_0000064205"
FT   DOMAIN          2..164
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   166 AA;  18025 MW;  57821688827B1123 CRC64;
     MSTVELNTSA GRIVLELNDA EAPKTVENFL AYVRSGHYDG TIFHRVISDF MIQGGGFTPD
     MQQKSTLAPI QNEADNGLRN DNYTVAMART NDPHSATAQF FINVKDNAFL NHTSKTPNGW
     GYAVFGRVTE GQDVVDAIKG VKTGSSRGHQ DVPVQPVVIE SAKILG