ID   PPIB_STRAQ              Reviewed;         175 AA.
AC   P77949;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase B;
DE            Short=PPIase B;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin ScCypB;
DE   AltName: Full=Rotamase B;
DE   AltName: Full=S-cyclophilin;
GN   Name=cypB;
OS   Streptomyces anulatus (Streptomyces chrysomallus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1892;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=9025285; DOI=10.1099/00221287-143-1-117;
RA   Pahl A., Gewies A., Keller U.;
RT   "ScCypB is a novel second cytosolic cyclophilin from Streptomyces
RT   chrysomallus which is phylogenetically distant from ScCypA.";
RL   Microbiology 143:117-126(1997).
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: Inhibited by cyclosporin A (CsA).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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DR   EMBL; U64692; AAB51775.1; -; Genomic_DNA.
DR   PIR; T51359; T51359.
DR   RefSeq; WP_050359820.1; NZ_CM003601.1.
DR   AlphaFoldDB; P77949; -.
DR   SMR; P77949; -.
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   InterPro; IPR044666; Cyclophilin_A-like.
DR   PANTHER; PTHR45625; PTHR45625; 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; Isomerase; Rotamase.
FT   CHAIN           1..175
FT                   /note="Peptidyl-prolyl cis-trans isomerase B"
FT                   /id="PRO_0000064207"
FT   DOMAIN          3..172
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   175 AA;  19017 MW;  E77616D34EFA5791 CRC64;
     MAEQLYATLK TNRGDIEIRL LPNHAPKTVR NFVELATGQR EWVNPETGEK STDRLYDGTV
     FHRVISGFMI QGGDPLGNGT GGPGYKFADE FHPELGFTQP YLLAMANAGP GTNGSQFFLT
     VSPTAWLTGK HTIFGEVSGE AGRKVVDAIA ATPTNPRTDR PLEDVVIESV VVETR