MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
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
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
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
- MyHits
| Description | RecName: 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 synonyms | PPIC_ECO57 , P0A9L7 , P39159 , 678A1BF2CBEA969B |
 Legends: 1, INIT_MET Removed. {ECO:0000250}; 2, ipat:PPIC_PPIASE_1 [T].
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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 02-NOV-2016, entry version 69.
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.,
RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA Welch R.A., 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.,
RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli
RT O157:H7 and 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
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; 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_LPWC02000002.1.
DR ProteinModelPortal; P0A9L7; -.
DR SMR; P0A9L7; -.
DR MINT; MINT-1225675; -.
DR STRING; 155864.Z5286; -.
DR EnsemblBacteria; AAG58970; AAG58970; Z5286.
DR EnsemblBacteria; BAB38132; BAB38132; BAB38132.
DR GeneID; 915269; -.
DR KEGG; ece:Z5286; -.
DR KEGG; ecs:ECs4709; -.
DR PATRIC; 18359027; VBIEscCol44059_4672.
DR eggNOG; ENOG4105KQ5; Bacteria.
DR eggNOG; COG0760; LUCA.
DR HOGENOM; HOG000275329; -.
DR KO; K03769; -.
DR OMA; GYHLIEI; -.
DR BioCyc; ECOO157:G7E-2-MONOMER; -.
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 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_0000193416.
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
//
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