ID   PPID_BUCAP              Reviewed;         621 AA.
AC   Q8K987;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Periplasmic chaperone PpiD {ECO:0000250|UniProtKB:P0ADY1};
DE   AltName: Full=Periplasmic folding chaperone {ECO:0000250|UniProtKB:P0ADY1};
GN   Name=ppiD; OrderedLocusNames=BUsg_462;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(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; AE013218; AAM68005.1; -; Genomic_DNA.
DR   RefSeq; WP_011053972.1; NC_004061.1.
DR   AlphaFoldDB; Q8K987; -.
DR   SMR; Q8K987; -.
DR   STRING; 198804.BUsg_462; -.
DR   GeneID; 75258657; -.
DR   KEGG; bas:BUsg_462; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_023843_1_1_6; -.
DR   Proteomes; UP000000416; Chromosome.
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   Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   PANTHER; PTHR47529; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE D; 1.
DR   PANTHER; PTHR47529:SF1; PERIPLASMIC CHAPERONE PPID; 1.
DR   Pfam; PF13145; Rotamase_2; 1.
DR   Pfam; PF13624; SurA_N_3; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 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..621
FT                   /note="Periplasmic chaperone PpiD"
FT                   /id="PRO_0000193421"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0ADY1"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..621
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0ADY1"
FT   DOMAIN          228..355
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
SQ   SEQUENCE   621 AA;  74140 MW;  5B7A89B253144C7C CRC64;
     MIKYLKSRLN IIIVKCILGI IILSLVFGTI NNYFNRDTTR YIAKVNGEEI SFITLQKMYI
     DERKKQEKIL GQDFEKIKKN KKFKEETYNY ILSQLINNIL LEQYTKRMNF NIQDNEIKKI
     IFNIPIFQEN NEFNKKKYLN YLSSKNLTHY EYVSLIRKKL NTTYLINAIS ETDFILDNEQ
     KKIIKLLSEK RIIKKAIIKI NPIINNQKVT EKEINNYFDQ HKNEFYTPEK FKISYIQLKP
     NKFKIQCSNE EIKNWYKKNI DKYSNQERRQ YSIIQTKTKN EALSILSELK KGEDFSKIAK
     EKSIDPFSSE QGGNIGWITK NFVPNEIKIA NLEKIDQISN IIKFNNNFLI IKLNKILPKK
     YKKISEVSDL IENEIKYQKS LNTYKKLKDK IAIIAKKNIN RFDLILKKTN ILPKETNWFD
     KDSVPKELQN PILKKIIFKK GLLDRQKKLK SHSGLIVLND HQSFLLSIKN FQKKRIKKLK
     DIKRNIVNKL KYIKAVEKTK NKLKKILFQL KIGNEHILKK ENIIFEEYET VSRYDKNPNI
     SVIFAMPHPK EEKNVYTMYQ NKNKNFVIAL LDKVYNEKFS NEEEKIIIKY LEKNNIDVTF
     QCFLQNLHRK ATILYNKTDN F
//