ID   PPID_BUCAI              Reviewed;         623 AA.
AC   P57550;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Periplasmic chaperone PpiD {ECO:0000250|UniProtKB:P0ADY1};
DE   AltName: Full=Periplasmic folding chaperone {ECO:0000250|UniProtKB:P0ADY1};
GN   Name=ppiD; OrderedLocusNames=BU478;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13175.1; -; Genomic_DNA.
DR   RefSeq; NP_240289.1; NC_002528.1.
DR   RefSeq; WP_010896137.1; NC_002528.1.
DR   AlphaFoldDB; P57550; -.
DR   SMR; P57550; -.
DR   STRING; 107806.10039141; -.
DR   EnsemblBacteria; BAB13175; BAB13175; BAB13175.
DR   KEGG; buc:BU478; -.
DR   PATRIC; fig|107806.10.peg.487; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_023843_1_1_6; -.
DR   OMA; DNSQGWI; -.
DR   Proteomes; UP000001806; 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; IPR027304; Trigger_fact/SurA_dom_sf.
DR   Pfam; PF13145; Rotamase_2; 1.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Chaperone; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..623
FT                   /note="Periplasmic chaperone PpiD"
FT                   /id="PRO_0000193420"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0ADY1"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..623
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0ADY1"
FT   DOMAIN          267..357
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
SQ   SEQUENCE   623 AA;  74262 MW;  3CF307543EBE01F6 CRC64;
     MTKYSQARLN SIIVKFILGV IILSLILSTI SIYINRDFEK YIATVNGEKI SFNLFKKMYF
     IEREKQKKIL GKNFFKFSHN ENFTKETYNY VLSQLINNVL LEQYAKNMNY LEVNDNTIKK
     IIYNSPIFQK NNKFSKERYL NYLTSINSTN HEYINIIKKK INTENLIHTI SKSNFILKKE
     EKNIIKLLSQ KRIIKKAIVK IDPSIYKKNI TNQEAQIYFK KNQDNFYIPE KFKINFVELK
     TDNFKIHCEN KEIYDWYIRN ITQYSTKEKR RYSIIQVKNK QQAISILSRL HNTPEDFSKI
     AQEQSTDPIS SKKDGDIGWI SIDLIPDEIK HANLNKKNQI SDVIPFHNEF LIVKLNETQI
     GTQKKIYEVF DSIKKQIKQK KSLDLYNELK NKISNNLKND PGKIERILKE NNILIQETDW
     FDKKSIPKVL NIPILKQFIF NKKLFQKDTT VKPQFHFIVL KKNQSFLIKI KKFKNKEIQH
     FENVKKNIIK KLRFIKAIKE TKKKSEEIIY DLTQGRKKLF KQSNLYFTDP EIISRYDLSA
     ITSIVFSLPH PQKGKKIYTL YNDKNKNFII ISLEKVYNTN FSEKEKNVIL EYLSRHNTEI
     IFNSILKDLR EKSIIKYENI VNK