ID   PPI1_STAES              Reviewed;         197 AA.
AC   Q8CT84;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Putative peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
GN   OrderedLocusNames=SE_0648;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04245.1; -; Genomic_DNA.
DR   RefSeq; NP_764203.1; NC_004461.1.
DR   RefSeq; WP_001831922.1; NZ_WBME01000044.1.
DR   AlphaFoldDB; Q8CT84; -.
DR   SMR; Q8CT84; -.
DR   STRING; 176280.SE_0648; -.
DR   EnsemblBacteria; AAO04245; AAO04245; SE_0648.
DR   GeneID; 50019205; -.
DR   KEGG; sep:SE_0648; -.
DR   PATRIC; fig|176280.10.peg.621; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_0_9; -.
DR   OMA; GEGYPGS; -.
DR   Proteomes; UP000001411; 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; 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; 2.
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   Isomerase; Rotamase.
FT   CHAIN           1..197
FT                   /note="Putative peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000299089"
FT   DOMAIN          14..195
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   197 AA;  21726 MW;  746F8877EE6F8FD4 CRC64;
     MTNYPQLNKE IQDNEIKVVM HTNKGDMTFK LFPDIAPKTV ENFVTHSKNG YYDGVTFHRV
     INDFMVQGGD PTATGMGGES IYGSAFEDEF SLEAFNLYGA LSMANAGPNT NGSQFFIVQM
     KEVPENMLSQ LADGGWPQPI VEAYGEKGGT PWLDQKHTVF GQLIEGESTL EDIANTKVGA
     QDKPVYDVVI ESIDVEE