ID   PPIA_ACIAD              Reviewed;         188 AA.
AC   P42693;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   Name=rotA; Synonyms=ppiA; OrderedLocusNames=ACIAD3647;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7948017; DOI=10.1016/0167-4781(94)90218-6;
RA   Kok R.G., Christoffels V.M., Vosman B., Hellingwerf K.J.;
RT   "A gene of Acinetobacter calcoaceticus BD413 encodes a periplasmic
RT   peptidyl-prolyl cis-trans isomerase of the cyclophilin sub-class that is
RT   not essential for growth.";
RL   Biochim. Biophys. Acta 1219:601-606(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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}.
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DR   EMBL; X74839; CAA52834.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG70278.1; -; Genomic_DNA.
DR   PIR; S50205; S50205.
DR   RefSeq; WP_004930172.1; NC_005966.1.
DR   AlphaFoldDB; P42693; -.
DR   SMR; P42693; -.
DR   STRING; 62977.ACIAD3647; -.
DR   EnsemblBacteria; CAG70278; CAG70278; ACIAD3647.
DR   GeneID; 45235810; -.
DR   KEGG; aci:ACIAD3647; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_9_6; -.
DR   OMA; VPFHRVM; -.
DR   OrthoDB; 1861282at2; -.
DR   BioCyc; ASP62977:ACIAD_RS16500-MON; -.
DR   Proteomes; UP000000430; 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..188
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000025499"
FT   DOMAIN          21..181
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   188 AA;  20398 MW;  A734EED2CEA13144 CRC64;
     MLKRVAIVLG GLLISAHALA NTMVEMKTNL GNIEIELYNN KAPISAKNFE SYVKNNFYNG
     TIFHRVIPNF MIQGGGFETN MKEKATAAPI KNEASNGLAN TRGTLAMART SNPDSATSQF
     FINVADNNFL NASRTDAGYA VFGKVIKGMD VVDKIANVPT STYGMHQNVP KQPVKIISVQ
     IKSINTAK