PPIC_ECO57
ID PPIC_ECO57 Reviewed; 93 AA.
AC P0A9L7; P39159;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 93.
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=Z5286, ECs4709;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG58970.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38132.1; -; Genomic_DNA.
DR PIR; E91217; E91217.
DR PIR; F86063; F86063.
DR RefSeq; NP_312736.1; NC_002695.1.
DR RefSeq; WP_001140251.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A9L7; -.
DR BMRB; P0A9L7; -.
DR SMR; P0A9L7; -.
DR STRING; 155864.EDL933_5096; -.
DR EnsemblBacteria; AAG58970; AAG58970; Z5286.
DR EnsemblBacteria; BAB38132; BAB38132; ECs_4709.
DR GeneID; 66672321; -.
DR GeneID; 915269; -.
DR KEGG; ece:Z5286; -.
DR KEGG; ecs:ECs_4709; -.
DR PATRIC; fig|386585.9.peg.4914; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_090028_6_1_6; -.
DR OMA; GPVRTQF; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; 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_0000193416"
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