(data stored in SCRATCH zone)

SWISSPROT: B7UKK2_ECO27

ID   B7UKK2_ECO27            Unreviewed;       164 AA.
AC   B7UKK2;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 67.
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:CAS08006.1};
GN   OrderedLocusNames=E2348C_0458 {ECO:0000313|EMBL:CAS08006.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08006.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08006.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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:
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         Evidence={ECO:0000256|RuleBase:RU363019};
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000256|RuleBase:RU363019}.
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DR   EMBL; FM180568; CAS08006.1; -; Genomic_DNA.
DR   RefSeq; WP_000255987.1; NC_011601.1.
DR   EnsemblBacteria; CAS08006; CAS08006; E2348C_0458.
DR   KEGG; ecg:E2348C_0458; -.
DR   HOGENOM; HOG000065978; -.
DR   KO; K03768; -.
DR   OMA; TSIYGQK; -.
DR   BioCyc; ECOL574521:E2348C_RS02400-MONOMER; -.
DR   Proteomes; UP000008205; 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_sf.
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; B7UKK2.
DR   SWISS-2DPAGE; B7UKK2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Isomerase {ECO:0000256|RuleBase:RU363019,
KW   ECO:0000313|EMBL:CAS08006.1};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN        1    162       PPIase cyclophilin-type.
FT                                {ECO:0000259|PROSITE:PS50072}.
SQ   SEQUENCE   164 AA;  18153 MW;  AD497C873B02C811 CRC64;
     MVTFHTNHGD IVIKTFDDKA PETVKNFLDY CREGFYNNTI FHRVINGFMI QGGGFEPGMK
     QKATKDPIKN EANNGLKNTR GTLAMARTQA PHSATAQFFI NVVDNDFLNF SGESLQGWGY
     CVFAEVVEGM DVVDKIKGVA TGRSGMHQDV PKEDVIIESV TVSE
//

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