ID   PPI1_STAS1              Reviewed;         197 AA.
AC   Q49W93;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Putative peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
GN   OrderedLocusNames=SSP1821;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE18966.1; -; Genomic_DNA.
DR   RefSeq; WP_002483798.1; NZ_MTGA01000039.1.
DR   AlphaFoldDB; Q49W93; -.
DR   SMR; Q49W93; -.
DR   STRING; 342451.SSP1821; -.
DR   EnsemblBacteria; BAE18966; BAE18966; SSP1821.
DR   GeneID; 66867995; -.
DR   KEGG; ssp:SSP1821; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_0_9; -.
DR   OMA; GEGYPGS; -.
DR   OrthoDB; 1861282at2; -.
DR   Proteomes; UP000006371; 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; Reference proteome; Rotamase.
FT   CHAIN           1..197
FT                   /note="Putative peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000299091"
FT   DOMAIN          14..195
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   197 AA;  21683 MW;  C32C660BCA758E3E CRC64;
     MTNYPQLNTE INGNEIKLIM HTNKGDMTFK LLPDVAPKTV ENFVTHAKNG YYNGVTFHRV
     INDFMVQGGD PTATGMGGES IYGEPFEDEF SKEAFNIYGA LSMANAGPHT NGSQFFIVQM
     NEVPESMLSQ LADGGWPEPI VKAYAETGGT PWLDQKHTVF GQLIEGKDTL EDIANTKVGP
     QDKPLHDITI DSIEIVE