ID   PPIA_MYCLE              Reviewed;         182 AA.
AC   Q9CDE9;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Probable peptidyl-prolyl cis-trans isomerase A;
DE            Short=PPIase A;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase A;
GN   Name=ppiA; OrderedLocusNames=ML0011;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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DR   EMBL; AL583917; CAC29519.1; -; Genomic_DNA.
DR   PIR; C86910; C86910.
DR   RefSeq; NP_301138.1; NC_002677.1.
DR   RefSeq; WP_010907463.1; NC_002677.1.
DR   AlphaFoldDB; Q9CDE9; -.
DR   SMR; Q9CDE9; -.
DR   STRING; 272631.ML0011; -.
DR   EnsemblBacteria; CAC29519; CAC29519; CAC29519.
DR   KEGG; mle:ML0011; -.
DR   PATRIC; fig|272631.5.peg.11; -.
DR   Leproma; ML0011; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_3_11; -.
DR   OMA; ELYNDHA; -.
DR   Proteomes; UP000000806; Chromosome.
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   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..182
FT                   /note="Probable peptidyl-prolyl cis-trans isomerase A"
FT                   /id="PRO_0000064208"
FT   DOMAIN          13..181
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          161..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   182 AA;  19367 MW;  6A6D8004348A9544 CRC64;
     MAHCDFVTNS LIQNATATLH TNRGDIKVAL FGNHVPKTVA NFVGLAQGTK EYSTQNASGG
     PSGPFYDGAV FHRVIQGFMI QGGDPTGTGR GGPGYKFADE FHPELQFDKP YLLAMANAGP
     GTNGSQFFIT VGETPHLNRR HTIFGEVTDP DSQKVVDAIS TTATDGNDRP TEPVVIDSIT
     IS