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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=Peptidyl-prolyl cis-trans isomerase C; Short=PPIase C; EC=5.2.1.8; AltName: Full=Parvulin; AltName: Full=Rotamase C;
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MyHits synonymsPPIC_ECOL6 , P0A9L6 , P39159 , 678A1BF2CBEA969B
match map segment
iprf:PPIC_PPIASE_2 ipat:PPIC_PPIASE_1  
Legends: 1, INIT_MET Removed. {ECO:0000250}; 2, ipat:PPIC_PPIASE_1 [T].
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   02-NOV-2016, entry version 66.
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.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of 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
CC       amino 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: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 PpiC domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00278}.
DR   EMBL; AE014075; AAN83129.1; -; Genomic_DNA.
DR   RefSeq; WP_001140251.1; NC_004431.1.
DR   ProteinModelPortal; P0A9L6; -.
DR   SMR; P0A9L6; -.
DR   STRING; 199310.c4697; -.
DR   EnsemblBacteria; AAN83129; AAN83129; c4697.
DR   KEGG; ecc:c4697; -.
DR   PATRIC; 18287081; VBIEscCol75197_4408.
DR   eggNOG; COG0760; LUCA.
DR   HOGENOM; HOG000275329; -.
DR   KO; K03769; -.
DR   OMA; GYHLIEI; -.
DR   BioCyc; ECOL199310:C4697-MONOMER; -.
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   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   Complete proteome; Cytoplasm; Isomerase; Rotamase.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2     93       Peptidyl-prolyl cis-trans isomerase C.
FT                                /FTId=PRO_0000193417.
FT   DOMAIN        2     91       PpiC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00278}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         2     91       iprf:PPIC_PPIASE_2 [T]
FT   MYHIT        31     51       ipat:PPIC_PPIASE_1 [T]
SQ   SEQUENCE   93 AA;  10232 MW;  678A1BF2CBEA969B CRC64;
     MAKTAAALHI LVKEEKLALD LLEQIKNGAD FGKLAKKHSI CPSGKRGGDL GEFRQGQMVP
     AFDKVVFSCP VLEPTGPLHT QFGYHIIKVL YRN
//