ID   PPID_ECOL6              Reviewed;         623 AA.
AC   P0ADY2; P77241;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Periplasmic chaperone PpiD {ECO:0000250|UniProtKB:P0ADY1};
DE   AltName: Full=Periplasmic folding chaperone {ECO:0000250|UniProtKB:P0ADY1};
GN   Name=ppiD; OrderedLocusNames=c0557;
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., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Chaperone that functions as a gatekeeper on the periplasmic
CC       side of the SecYEG translocon. Facilitates the translocation of
CC       precursor proteins across SecYEG by interacting with the translocating
CC       substrate. Also plays a role in the release of newly synthesized
CC       secreted proteins at the periplasmic exit site of the Sec translocon.
CC       {ECO:0000250|UniProtKB:P0ADY1}.
CC   -!- SUBUNIT: Interacts with the SecYEG translocon (By similarity). Binds to
CC       the lateral gate of SecY (By similarity). Forms a complex with YfgM (By
CC       similarity). {ECO:0000250|UniProtKB:P0ADY1}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P0ADY1}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:P0ADY1}; Periplasmic side
CC       {ECO:0000250|UniProtKB:P0ADY1}. Note=Located at the lateral gate of
CC       SecY. {ECO:0000250|UniProtKB:P0ADY1}.
CC   -!- SIMILARITY: Belongs to the PpiD chaperone family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN79035.1; -; Genomic_DNA.
DR   RefSeq; WP_000969372.1; NC_004431.1.
DR   AlphaFoldDB; P0ADY2; -.
DR   BMRB; P0ADY2; -.
DR   SMR; P0ADY2; -.
DR   STRING; 199310.c0557; -.
DR   PRIDE; P0ADY2; -.
DR   EnsemblBacteria; AAN79035; AAN79035; c0557.
DR   KEGG; ecc:c0557; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_023843_1_1_6; -.
DR   OMA; DNSQGWI; -.
DR   BioCyc; ECOL199310:C0557-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Chaperone; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..623
FT                   /note="Periplasmic chaperone PpiD"
FT                   /id="PRO_0000193424"
FT   TOPO_DOM        1..15
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0ADY1"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..623
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0ADY1"
FT   DOMAIN          266..355
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
SQ   SEQUENCE   623 AA;  68150 MW;  0F646F687114A387 CRC64;
     MMDSLRTAAN SLVLKIIFGI IIVSFILTGV SGYLIGGGNN YAAKVNDQEI SRGQFENAFN
     SERNRMQQQL GDQYSELAAN EGYMKTLRQQ 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