ID   PPI1_STAA3              Reviewed;         197 AA.
AC   Q2FIC1;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Putative peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
GN   OrderedLocusNames=SAUSA300_0857;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
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; CP000255; ABD20840.1; -; Genomic_DNA.
DR   RefSeq; WP_000035058.1; NZ_CP027476.1.
DR   AlphaFoldDB; Q2FIC1; -.
DR   SMR; Q2FIC1; -.
DR   EnsemblBacteria; ABD20840; ABD20840; SAUSA300_0857.
DR   KEGG; saa:SAUSA300_0857; -.
DR   HOGENOM; CLU_012062_16_0_9; -.
DR   OMA; GEGYPGS; -.
DR   BRENDA; 5.2.1.8; 3352.
DR   Proteomes; UP000001939; 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; IPR024936; Cyclophilin-type_PPIase.
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; 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_0000299079"
FT   DOMAIN          14..195
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   197 AA;  21619 MW;  71F2FE0713702B34 CRC64;
     MANYPQLNKE VQQGEIKVVM HTNKGDMTFK LFPNIAPKTV ENFVTHAKNG YYDGITFHRV
     INDFMIQGGD PTATGMGGES IYGGAFEDEF SLNAFNLYGA LSMANSGPNT NGSQFFIVQM
     KEVPQNMLSQ LADGGWPQPI VDAYGEKGGT PWLDQKHTVF GQIIDGETTL EDIANTKVGP
     QDKPLHDVVI ESIDVEE