ID   PPIA_DICD3              Reviewed;         190 AA.
AC   O53021; E0SJQ9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase A;
DE            Short=PPIase A;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin A;
DE   AltName: Full=Rotamase A;
DE   Flags: Precursor;
GN   Name=rotA; Synonyms=ppiA; OrderedLocusNames=Dda3937_04190;
OS   Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=198628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=3937;
RX   PubMed=9418240; DOI=10.1111/j.1574-6968.1997.tb12753.x;
RA   Pissavin C., Hugouvieux-Cotte-Pattat N.;
RT   "Characterization of a periplasmic peptidyl-prolyl cis-trans isomerase in
RT   Erwinia chrysanthemi.";
RL   FEMS Microbiol. Lett. 157:59-65(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3937;
RX   PubMed=21217001; DOI=10.1128/jb.01513-10;
RA   Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA   Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA   Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA   Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA   Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA   Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA   Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA   Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA   Blattner F.R., Keen N.T., Perna N.T.;
RT   "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL   J. Bacteriol. 193:2076-2077(2011).
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   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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DR   EMBL; Y09804; CAA70935.1; -; Genomic_DNA.
DR   EMBL; CP002038; ADN00348.1; -; Genomic_DNA.
DR   RefSeq; WP_013319748.1; NC_014500.1.
DR   AlphaFoldDB; O53021; -.
DR   SMR; O53021; -.
DR   STRING; 198628.Dda3937_04190; -.
DR   EnsemblBacteria; ADN00348; ADN00348; Dda3937_04190.
DR   GeneID; 9735634; -.
DR   KEGG; ddd:Dda3937_04190; -.
DR   PATRIC; fig|198628.6.peg.4090; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_9_6; -.
DR   OMA; VPFHRVM; -.
DR   OrthoDB; 1861282at2; -.
DR   BioCyc; DDAD198628:DDA3937_RS19510-MON; -.
DR   Proteomes; UP000006859; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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.
PE   3: Inferred from homology;
KW   Isomerase; Periplasm; Reference proteome; Rotamase; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..190
FT                   /note="Peptidyl-prolyl cis-trans isomerase A"
FT                   /id="PRO_0000025500"
FT   DOMAIN          26..187
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   CONFLICT        8
FT                   /note="A -> P (in Ref. 1; CAA70935)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="S -> F (in Ref. 1; CAA70935)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   190 AA;  20476 MW;  08527651DB393F59 CRC64;
     MSKRILAAVV TVLSLTAFSP AFAATTSTHV LLTTSAGNIE LALDDQKAPV SVKNFVDYVN
     SGFYNGTIFH RVIPGFMVQG GGFSSDMKQK ATNPPVKNEA DNGLRNLRGT ISMARTSEKD
     SATSQFFINV ADNAFLDHGQ RDFGYAVFGK VVKGMEVADK ISQVQTENVG PYQNVPSKPI
     VIQSAKIIKK