ID   PPIB_MYCLE              Reviewed;         295 AA.
AC   P46697;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Probable peptidyl-prolyl cis-trans isomerase B;
DE            Short=PPIase B;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase B;
GN   Name=ppiB; Synonyms=ppi; OrderedLocusNames=ML0492;
GN   ORFNames=B1177_F3_97, MLCB1259.10c;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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; U00011; AAA17113.1; -; Genomic_DNA.
DR   EMBL; AL023591; CAA19085.1; -; Genomic_DNA.
DR   EMBL; AL583918; CAC30000.1; -; Genomic_DNA.
DR   PIR; S72749; S72749.
DR   RefSeq; NP_301431.1; NC_002677.1.
DR   RefSeq; WP_010907755.1; NC_002677.1.
DR   AlphaFoldDB; P46697; -.
DR   SMR; P46697; -.
DR   STRING; 272631.ML0492; -.
DR   EnsemblBacteria; CAC30000; CAC30000; CAC30000.
DR   KEGG; mle:ML0492; -.
DR   PATRIC; fig|272631.5.peg.856; -.
DR   Leproma; ML0492; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_8_0_11; -.
DR   OMA; SKAPDPC; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
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; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044666; Cyclophilin_A-like.
DR   PANTHER; PTHR45625; PTHR45625; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..295
FT                   /note="Probable peptidyl-prolyl cis-trans isomerase B"
FT                   /id="PRO_0000064211"
FT   DOMAIN          126..294
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          105..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   295 AA;  31178 MW;  141B86944A34B5D1 CRC64;
     MPTNEQRRAT AKRKLKRQLE RRAKQARWRR VLLISGGVVV AVAVIITVVA TVVISKLGHK
     HDTASSTASN SLTATKTPAV TPSVLPLPSF QPSTNLGVNC QYPPSADKAA KPVKPPRAGK
     VPTDPATVSA SMATNQGNIG LLLNNAESPC TVNSFASLTG QGFFNNTKCH RLTTSLMLGV
     LQCGDPKVDG TGGPGYKFAN EYPTDQYPPN DPKLKQPVLY PRGTLAMANS GPNTNGSQFF
     LVYHDSQLPP EYTVFGTIQA DGLATLDKIA KGGIASGGDD GPPATEVTIE SLRLD