ID   PPIA_PSEAE              Reviewed;         187 AA.
AC   Q59641; Q9HZ13;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 127.
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=ppiA; Synonyms=cypH; OrderedLocusNames=PA3227;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-175.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=8581173; DOI=10.1099/13500872-142-1-79;
RA   Liao X., Charlebois I., Ouellet C., Morency M.J., Dewar K., Lightfoot J.,
RA   Foster J., Siehnel R., Schweizer H., Lam J.S., Hancock R.E., Levesque R.C.;
RT   "Physical mapping of 32 genetic markers on the Pseudomonas aeruginosa PAO1
RT   chromosome.";
RL   Microbiology 142:79-86(1996).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. This protein is not essential for growth. Presumably
CC       plays a role in signal transduction.
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 {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004091; AAG06615.1; -; Genomic_DNA.
DR   EMBL; X84050; CAA58868.1; -; Genomic_DNA.
DR   PIR; G83243; G83243.
DR   RefSeq; NP_251917.1; NC_002516.2.
DR   RefSeq; WP_003114812.1; NZ_QZGE01000019.1.
DR   AlphaFoldDB; Q59641; -.
DR   SMR; Q59641; -.
DR   STRING; 287.DR97_4708; -.
DR   PaxDb; Q59641; -.
DR   PRIDE; Q59641; -.
DR   DNASU; 882464; -.
DR   EnsemblBacteria; AAG06615; AAG06615; PA3227.
DR   GeneID; 882464; -.
DR   KEGG; pae:PA3227; -.
DR   PATRIC; fig|208964.12.peg.3374; -.
DR   PseudoCAP; PA3227; -.
DR   HOGENOM; CLU_012062_16_9_6; -.
DR   InParanoid; Q59641; -.
DR   OMA; MRAPIVN; -.
DR   PhylomeDB; Q59641; -.
DR   BioCyc; PAER208964:G1FZ6-3286-MON; -.
DR   Proteomes; UP000002438; 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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..187
FT                   /note="Peptidyl-prolyl cis-trans isomerase A"
FT                   /id="PRO_0000025501"
FT   DOMAIN          25..186
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   CONFLICT        22..24
FT                   /note="TPA -> GTT (in Ref. 2; CAA58868)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        173..174
FT                   /note="DV -> SL (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   187 AA;  20104 MW;  5664DBC83FB94594 CRC64;
     MLKRLLIAAC TLLFAGSLLA ATPAAKPHVL IATSLGEIEV ELDPAKAPIS VKNFLEYVDS
     GYYDGTLFHR VIPGFMVQTG GFSAGMQEKK TRAPIKNEAD NGLLNERGTL AMARTGVVDS
     ATSQFFINLT DNDFLNHGAR DFGYAVFGKV VRGMGVVDQI AKVPTTRRNG FADVPSDDVV
     ILSAKRL