(data stored in ACNUC7421 zone)

SWISSPROT: Q8XCU0_ECO57

ID   Q8XCU0_ECO57            Unreviewed;       164 AA.
AC   Q8XCU0; Q7AGU3;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 127.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE            Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN   Name=ppiB {ECO:0000313|EMBL:AAG54882.1};
GN   OrderedLocusNames=ECs0587 {ECO:0000313|EMBL:BAB34010.1}, Z0680
GN   {ECO:0000313|EMBL:AAG54882.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|Proteomes:UP000002519};
RN   [1] {ECO:0000313|EMBL:BAB34010.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558}, and Sakai
RC   {ECO:0000313|EMBL:BAB34010.1};
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., 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).
RN   [2] {ECO:0000313|EMBL:AAG54882.1, ECO:0000313|Proteomes:UP000002519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EDL933 {ECO:0000313|EMBL:AAG54882.1}, and O157:H7 / EDL933 /
RC   ATCC 700927 / EHEC {ECO:0000313|Proteomes:UP000002519};
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., 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).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. {ECO:0000256|RuleBase:RU363019}.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0). {ECO:0000256|RuleBase:RU363019}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000256|RuleBase:RU363019}.
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DR   EMBL; AE005174; AAG54882.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34010.1; -; Genomic_DNA.
DR   PIR; C90702; C90702.
DR   PIR; F85552; F85552.
DR   RefSeq; NP_308614.1; NC_002695.1.
DR   RefSeq; WP_000256002.1; NZ_MWVM01000032.1.
DR   ProteinModelPortal; Q8XCU0; -.
DR   STRING; 155864.Z0680; -.
DR   EnsemblBacteria; AAG54882; AAG54882; Z0680.
DR   EnsemblBacteria; BAB34010; BAB34010; BAB34010.
DR   GeneID; 916942; -.
DR   KEGG; ece:Z0680; -.
DR   KEGG; ecs:ECs0587; -.
DR   PATRIC; fig|386585.9.peg.694; -.
DR   eggNOG; ENOG4108R5K; Bacteria.
DR   eggNOG; COG0652; LUCA.
DR   HOGENOM; HOG000065978; -.
DR   KO; K03768; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8XCU0.
DR   SWISS-2DPAGE; Q8XCU0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558,
KW   ECO:0000313|Proteomes:UP000002519};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00156,
KW   ECO:0000256|RuleBase:RU363019, ECO:0000313|EMBL:AAG54882.1};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00156,
KW   ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN        1    162       PPIase cyclophilin-type.
FT                                {ECO:0000259|PROSITE:PS50072}.
SQ   SEQUENCE   164 AA;  18167 MW;  4D5C7D2D8AA9D2A0 CRC64;
     MVTFHTNHGD IVIKTFDDKA PETVKNFLDY CREGFYNNTI FHRVINGFMI QGGGFEPGMK
     QKATKEPIKN EANNGLKNTR GTLAMARTQA PHSATAQFFI NVVDNDFLNF SGESLQGWGY
     CVFAEVVEGM DVVDKIKGVA TGRSGMHQDV PKEDVIIESV TVSE
//

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