ID   PPIA_SALTY              Reviewed;         190 AA.
AC   P20753;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   19-DEC-2001, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase A;
DE            Short=PPIase A;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase A;
DE   Flags: Precursor;
GN   Name=ppiA; Synonyms=rot, rotA; OrderedLocusNames=STM3472;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-190.
RX   PubMed=2403545; DOI=10.1128/jb.172.1.397-410.1990;
RA   Tran P.V., Bannor T.A., Doktor S.Z., Nichols B.P.;
RT   "Chromosomal organization and expression of Escherichia coli pabA.";
RL   J. Bacteriol. 172:397-410(1990).
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   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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DR   EMBL; AE006468; AAL22334.1; -; Genomic_DNA.
DR   EMBL; M32355; AAA27174.1; -; Genomic_DNA.
DR   RefSeq; NP_462375.1; NC_003197.2.
DR   RefSeq; WP_000920478.1; NC_003197.2.
DR   AlphaFoldDB; P20753; -.
DR   BMRB; P20753; -.
DR   SMR; P20753; -.
DR   STRING; 99287.STM3472; -.
DR   PaxDb; P20753; -.
DR   EnsemblBacteria; AAL22334; AAL22334; STM3472.
DR   GeneID; 1254995; -.
DR   KEGG; stm:STM3472; -.
DR   PATRIC; fig|99287.12.peg.3669; -.
DR   HOGENOM; CLU_012062_16_9_6; -.
DR   OMA; VPFHRVM; -.
DR   PhylomeDB; P20753; -.
DR   BioCyc; SENT99287:STM3472-MON; -.
DR   Proteomes; UP000001014; 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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..190
FT                   /note="Peptidyl-prolyl cis-trans isomerase A"
FT                   /id="PRO_0000025498"
FT   DOMAIN          27..188
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   CONFLICT        45..46
FT                   /note="NS -> DK (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54
FT                   /note="K -> Q (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="N -> T (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   190 AA;  20332 MW;  B2A14BF20B02E4B0 CRC64;
     MLKSTLAAVA AVFALSALSP AALAAKGDPH VLLTTSAGNI ELELNSQKAP VSVKNFVDYV
     NSGFYNNTTF HRVIPGFMIQ GGGFNEQMQQ KKPNPPIKNE ADNGLRNTRG TIAMARTADK
     DSATSQFFIN VADNAFLDHG QRDFGYAVFG KVVKGMDVAD KISQVPTHDV GPYQNVPTKP
     VVILSAKVLP