ID   PPI1_SYNY3              Reviewed;         246 AA.
AC   P72704;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Probable peptidyl-prolyl cis-trans isomerase sll0227;
DE            Short=PPIase sll0227;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase sll0227;
DE   Flags: Precursor;
GN   OrderedLocusNames=sll0227;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
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; BA000022; BAA16711.1; -; Genomic_DNA.
DR   PIR; S74559; S74559.
DR   AlphaFoldDB; P72704; -.
DR   SMR; P72704; -.
DR   STRING; 1148.1651784; -.
DR   PaxDb; P72704; -.
DR   PRIDE; P72704; -.
DR   EnsemblBacteria; BAA16711; BAA16711; BAA16711.
DR   KEGG; syn:sll0227; -.
DR   eggNOG; COG0652; Bacteria.
DR   InParanoid; P72704; -.
DR   OMA; DYAVFGY; -.
DR   PhylomeDB; P72704; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; HDA:UniProtKB.
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; IPR044665; E_coli_cyclophilin_A-like.
DR   PANTHER; PTHR43246; PTHR43246; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome; Rotamase; Signal.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           37..246
FT                   /note="Probable peptidyl-prolyl cis-trans isomerase
FT                   sll0227"
FT                   /id="PRO_0000025502"
FT   DOMAIN          64..246
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          31..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   246 AA;  26580 MW;  02080EE3C339932F CRC64;
     MRILPNISRA TWFVGIFFVV NILLTACNQP SANSSAEPSP TETNSPVAQV TTDPYKDYKP
     RLNGKATVEM MVNGQPIIIE VDGENAPITA GNFVDLVEQG FYNGLTFHRV VDGFVAQGGD
     PKGDGTGGYV DKNTQRPRNI PLEIKVDPAV ENAPETPVYS RALGNQAGFP VMLPHKTGAV
     AMARSQMPDS ASSQFYFTLS DETGFLDGDY AVFGYVTQGM DVVLKIKQGD KIQSAKVITG
     QNNLEK