ID   PPIB_ORPSP              Reviewed;         203 AA.
AC   Q01490;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase B;
DE            Short=PPIase B;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin B;
DE   AltName: Full=Rotamase B;
DE   Flags: Precursor;
GN   Name=CYPB;
OS   Orpinomyces sp. (strain PC-2).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Orpinomyces; unclassified Orpinomyces.
OX   NCBI_TaxID=50059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 23-52.
RX   PubMed=7708690; DOI=10.1073/pnas.92.7.2587;
RA   Chen H., Li X.-L., Ljungdahl L.G.;
RT   "A cyclophilin from the polycentric anaerobic rumen fungus Orpinomyces sp.
RT   strain PC-2 is highly homologous to vertebrate cyclophilin B.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:2587-2591(1995).
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: Endoplasmic reticulum lumen {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U17900; AAD04195.1; -; mRNA.
DR   AlphaFoldDB; Q01490; -.
DR   SMR; Q01490; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; 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   Direct protein sequencing; Endoplasmic reticulum; Isomerase; Rotamase;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:7708690"
FT   CHAIN           23..203
FT                   /note="Peptidyl-prolyl cis-trans isomerase B"
FT                   /id="PRO_0000025485"
FT   DOMAIN          33..190
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   MOTIF           200..203
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="cyclosporin A"
FT                   /ligand_id="ChEBI:CHEBI:4031"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   203 AA;  21969 MW;  A5748C94305B8BE0 CRC64;
     MNFSIKSVIF LAIVALATLV SASTNPKVTN KVYFDIKQGD KDLGRIVLGL YGEVVPKTVE
     NFRALATGEK GYGYKNSKFH RVIKDFMIQG GDFTRGDGTG GKSIYGERFA DENFKLRHTG
     PGILSMANAG RDTNGSQFFI TTVTTSWLDG RHVVFGKVIE GMDVVTAIET TKTLPGDRPA
     TPVIIADCGE LPVSNNNDAK AEL