ID   PPI_SYNE7               Reviewed;         145 AA.
AC   P29820; Q31NA8;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
GN   Name=rot; OrderedLocusNames=Synpcc7942_1431;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kaplan A.;
RL   Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; X65028; CAA46162.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57461.1; -; Genomic_DNA.
DR   PIR; S19922; CSYC42.
DR   RefSeq; WP_011242439.1; NC_007604.1.
DR   AlphaFoldDB; P29820; -.
DR   SMR; P29820; -.
DR   STRING; 1140.Synpcc7942_1431; -.
DR   PRIDE; P29820; -.
DR   EnsemblBacteria; ABB57461; ABB57461; Synpcc7942_1431.
DR   KEGG; syf:Synpcc7942_1431; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_4_3; -.
DR   OMA; VPFHRVM; -.
DR   OrthoDB; 1861282at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1431-MON; -.
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; 1.
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..145
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000064201"
FT   DOMAIN          1..145
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   145 AA;  15657 MW;  C6D36FD2703B4079 CRC64;
     MTQAILETEK GTIRLQFFDN DAPNTVANFV KLSQDGFYDG LTFHRVIPGF MSQGGCPHGT
     GTGGPGYKIP CEINDNPHLA GTLSMAHAGR NTGGSQFFIC HEPQPHLDGV HTTFGQTEDD
     ESLKVVRSLR NGDRILSVKI VTDAA