ID   PPIB_TREPA              Reviewed;         215 AA.
AC   O66105;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Probable peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
GN   Name=ppiB; Synonyms=ppi; OrderedLocusNames=TP_0947;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=9317025; DOI=10.1128/iai.65.10.4179-4189.1997;
RA   Shevchenko D.V., Akins D.R., Robinson E.J., Li M., Shevchenko O.V.,
RA   Radolf J.D.;
RT   "Identification of homologs for thioredoxin, peptidyl prolyl cis-trans
RT   isomerase, and glycerophosphodiester phosphodiesterase in outer membrane
RT   fractions from Treponema pallidum, the syphilis spirochete.";
RL   Infect. Immun. 65:4179-4189(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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}.
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DR   EMBL; U97573; AAC08055.1; -; Genomic_DNA.
DR   EMBL; AE000520; AAC65904.1; -; Genomic_DNA.
DR   PIR; A71261; A71261.
DR   RefSeq; WP_010882390.1; NC_021490.2.
DR   AlphaFoldDB; O66105; -.
DR   SMR; O66105; -.
DR   IntAct; O66105; 14.
DR   STRING; 243276.TPANIC_0947; -.
DR   EnsemblBacteria; AAC65904; AAC65904; TP_0947.
DR   KEGG; tpa:TP_0947; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_4_12; -.
DR   OMA; VPFHRVM; -.
DR   OrthoDB; 1861282at2; -.
DR   Proteomes; UP000000811; Chromosome.
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; 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   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; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..215
FT                   /note="Probable peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000064213"
FT   DOMAIN          38..197
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   215 AA;  23272 MW;  CCA1589C1F5A6D0B CRC64;
     MNTQVWRVCV GVMLFCFVGR IGCAEEKMVR EEGLAVADGI YAVMETNRGT IVLSLFFEKA
     PLTVCNFVGL AEGTLAVCKG RPFYQGLTFH RVIKDFMIQG GDPQGNGTGG PGYQFPDECD
     PALRHDSPGV LSMANAGPGT NGSQFFITHV ATPWLDGKHT VFGKVVEGME VVHAIIAGDT
     IRSLKIVRRG AAAKRFVCDQ AQFDQLRKRV SAASK