(data stored in SCRATCH zone)

SWISSPROT: B7UJR4_ECO27

ID   B7UJR4_ECO27            Unreviewed;       623 AA.
AC   B7UJR4;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Peptidylprolyl isomerase {ECO:0000256|SAAS:SAAS00143148};
DE            EC=5.2.1.8 {ECO:0000256|SAAS:SAAS00143148};
GN   Name=ppiD {ECO:0000313|EMBL:CAS07924.1};
GN   OrderedLocusNames=E2348C_0376 {ECO:0000313|EMBL:CAS07924.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07924.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07924.1, 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   -!- 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|SAAS:SAAS01128631};
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DR   EMBL; FM180568; CAS07924.1; -; Genomic_DNA.
DR   RefSeq; WP_000969352.1; NC_011601.1.
DR   EnsemblBacteria; CAS07924; CAS07924; E2348C_0376.
DR   KEGG; ecg:E2348C_0376; -.
DR   HOGENOM; HOG000276975; -.
DR   KO; K03770; -.
DR   OMA; SQGWIAK; -.
DR   BioCyc; ECOL574521:E2348C_RS01975-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   Pfam; PF13145; Rotamase_2; 1.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   4: Predicted;
DR   PRODOM; B7UJR4.
DR   SWISS-2DPAGE; B7UJR4.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|SAAS:SAAS00143328, ECO:0000313|EMBL:CAS07924.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000256|SAAS:SAAS00143327};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     12     35       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      266    355       PpiC. {ECO:0000259|PROSITE:PS50198}.
FT   COILED      479    499       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   623 AA;  68163 MW;  0F60BD42F76EA387 CRC64;
     MMDSLRTAAN SLVLKIIFGI IIVSFILTGV SGYLIGGGNN YAAKVNDQEI SRGQFENAFN
     SERNRMQQQL GDQYSELAAN EGYMKNLRQQ VLNRLIDEAL LDQYARELKL GISDEQVKQA
     IFATPAFQVD GKFDNSRYNG ILNQMGMTAD QYAQALRNQL TTQQLINGVA GTDFMLKGET
     DELAALVAQQ RVVREATIDV NALAAKQPVT EQEIASYYEQ NKNNFMTPEQ FRVSYIKLDA
     ATMQQPVSDA DIQSYYDQHQ DQFTQPQRTR YSIIQTKTED EAKAVLDELN KGGDFAALAK
     EKSADIISAR NGGDMGWLED ATIPDELKNA GLKEKGQLSG VIKSSVGFLI VRLDDIQPAK
     VKSLDEVRDD IAAKVKHEKA LDAYYALQQK VSDAASNDTE SLAGAEQAAG VKATQTGWFS
     KDNLPEELNF KPVADAIFNG GLVGENGAPG INSDIITVDG DRAFVLRISE HKPEAVKPLA
     DVQEQVKALV QHNKAEQQAK VDAEKLLVDL KAGKGAEAMQ AAGLKFGEPK TLSRSGRDPI
     SQAAFALPLP AKDKPSYGMA TDMQGNVVLL ALDEVKQGSM PEDQKKAMVQ GITQNNAQIV
     FEALMSNLRK EAKIKIGDAL EQQ
//

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