ID   PPIC_SALTI              Reviewed;          93 AA.
AC   P0A266; Q9L6S3;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase C;
DE            Short=PPIase C;
DE            EC=5.2.1.8;
DE   AltName: Full=Parvulin;
DE   AltName: Full=Rotamase C;
GN   Name=ppiC; OrderedLocusNames=STY3647, t3388;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It prefers amino
CC       acid residues with hydrophobic side chains like leucine and
CC       phenylalanine in the P1 position of the peptides substrates (By
CC       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: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC       {ECO:0000305}.
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DR   EMBL; AL513382; CAD09407.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO70912.1; -; Genomic_DNA.
DR   RefSeq; NP_457838.1; NC_003198.1.
DR   RefSeq; WP_001096806.1; NZ_WSUR01000032.1.
DR   AlphaFoldDB; P0A266; -.
DR   SMR; P0A266; -.
DR   STRING; 220341.16504525; -.
DR   EnsemblBacteria; AAO70912; AAO70912; t3388.
DR   KEGG; stt:t3388; -.
DR   KEGG; sty:STY3647; -.
DR   PATRIC; fig|220341.7.peg.3716; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_090028_6_1_6; -.
DR   OMA; GPVRTQF; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR023058; PPIase_PpiC_CS.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Rotamase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..93
FT                   /note="Peptidyl-prolyl cis-trans isomerase C"
FT                   /id="PRO_0000193418"
FT   DOMAIN          2..91
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
SQ   SEQUENCE   93 AA;  10328 MW;  DB929A1FF00EB0F0 CRC64;
     MAKMAAALHI LVKEEKLALD LLEQIKNGGD FEKLAKKHSI CPSGKKGGHL GEFRQGQMVP
     AFDKVVFSCP VLEPTGPLHT QFGYHIIKVL YRK