ID   PPI1_STAHJ              Reviewed;         198 AA.
AC   Q4L4W9;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Putative peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
GN   OrderedLocusNames=SH1997;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(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; AP006716; BAE05306.1; -; Genomic_DNA.
DR   RefSeq; WP_011276264.1; NC_007168.1.
DR   AlphaFoldDB; Q4L4W9; -.
DR   SMR; Q4L4W9; -.
DR   STRING; 279808.SH1997; -.
DR   EnsemblBacteria; BAE05306; BAE05306; SH1997.
DR   KEGG; sha:SH1997; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_0_9; -.
DR   OMA; GEGYPGS; -.
DR   OrthoDB; 1861282at2; -.
DR   Proteomes; UP000000543; 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..198
FT                   /note="Putative peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000299090"
FT   DOMAIN          14..195
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   198 AA;  21726 MW;  2ACB9119CCE9C78A CRC64;
     MTNYPQLNKE IQDNEIKVAM HTNKGDMTFK LFPDIAPKTV ENFVTHAKNG YYDGITFHRV
     INDFMIQGGD PTATGMGGES IYGGSFEDEF SLEAFNLYGA LSMANAGPNT NGSQFFVVQM
     KEVPESMVNQ LVDGGWPEPI AKAYADNGGT PWLDQKHTVF GQLIEGEATL EDIANTKVGA
     QDKPVHDVVI ESIDVEDK