ID   FKBP_STRAQ              Reviewed;         124 AA.
AC   P28725;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=FK506-binding protein;
DE            EC=5.2.1.8;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE   AltName: Full=Rotamase;
GN   Name=fkbP;
OS   Streptomyces anulatus (Streptomyces chrysomallus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1892;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-36.
RC   STRAIN=ATCC 11523 / DSM 40128 / JCM 4296 / LMG 20459 / NBRC 15393;
RX   PubMed=1381710; DOI=10.1128/jb.174.18.5888-5894.1992;
RA   Pahl A., Keller U.;
RT   "FK-506-binding proteins from streptomycetes producing immunosuppressive
RT   macrolactones of the FK-506 type.";
RL   J. Bacteriol. 174:5888-5894(1992).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins.
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 FK506, ascomycin and rapamycin.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   EMBL; M98428; AAA26745.1; -; Genomic_DNA.
DR   PIR; A43328; A43328.
DR   RefSeq; WP_050359483.1; NZ_CM003601.1.
DR   AlphaFoldDB; P28725; -.
DR   SMR; P28725; -.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR044609; FKBP2/11.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR45779; PTHR45779; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Isomerase; Rotamase.
FT   CHAIN           1..124
FT                   /note="FK506-binding protein"
FT                   /id="PRO_0000075354"
FT   DOMAIN          35..124
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   124 AA;  12936 MW;  82B9EEAA2B7DD5A2 CRC64;
     MSIEKPEVDF PGGEPPADLA IKDIWEGDGP VAQAGQTVSV HYVGVAFSTG EEFDASWNRG
     TPLQFQLGAG QVISGWDQGV QGMKVGGRRE LIIPAHLAYG DRGAGGGKIA PGETLIFVCD
     LVAV