ID   PPIC_ECOL6              Reviewed;          93 AA.
AC   P0A9L6; P39159;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 84.
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=c4697;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN83129.1; -; Genomic_DNA.
DR   RefSeq; WP_001140251.1; NC_004431.1.
DR   AlphaFoldDB; P0A9L6; -.
DR   BMRB; P0A9L6; -.
DR   SMR; P0A9L6; -.
DR   STRING; 199310.c4697; -.
DR   EnsemblBacteria; AAN83129; AAN83129; c4697.
DR   GeneID; 66672321; -.
DR   KEGG; ecc:c4697; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_090028_6_1_6; -.
DR   OMA; GPVRTQF; -.
DR   BioCyc; ECOL199310:C4697-MON; -.
DR   Proteomes; UP000001410; 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_0000193417"
FT   DOMAIN          2..91
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
SQ   SEQUENCE   93 AA;  10232 MW;  678A1BF2CBEA969B CRC64;
     MAKTAAALHI LVKEEKLALD LLEQIKNGAD FGKLAKKHSI CPSGKRGGDL GEFRQGQMVP
     AFDKVVFSCP VLEPTGPLHT QFGYHIIKVL YRN