ID   PPID_BUCBP              Reviewed;         511 AA.
AC   Q89A98;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Putative chaperone PpiD {ECO:0000250|UniProtKB:P0ADY1};
GN   Name=ppiD; OrderedLocusNames=bbp_422;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC   -!- FUNCTION: Chaperone that functions as a gatekeeper on the extracellular
CC       side of the Sec translocon. Facilitates the translocation of precursor
CC       proteins across Sec by interacting with the translocating substrate.
CC       Also plays a role in the release of newly synthesized secreted proteins
CC       at the extracellular exit site of the Sec translocon.
CC       {ECO:0000250|UniProtKB:P0ADY1}.
CC   -!- SUBUNIT: Interacts with the Sec 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 membrane {ECO:0000250|UniProtKB:P0ADY1};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:P0ADY1};
CC       Extracellular side {ECO:0000250|UniProtKB:P0ADY1}. Note=Located at the
CC       lateral gate of SecY. {ECO:0000250|UniProtKB:P0ADY1}.
CC   -!- SIMILARITY: Belongs to the PpiD chaperone family. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. Contains an internal
CC       deletion relative to its orthologs. {ECO:0000305}.
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DR   EMBL; AE016826; AAO27132.1; -; Genomic_DNA.
DR   RefSeq; WP_011091533.1; NC_004545.1.
DR   AlphaFoldDB; Q89A98; -.
DR   STRING; 224915.bbp_422; -.
DR   EnsemblBacteria; AAO27132; AAO27132; bbp_422.
DR   GeneID; 56470957; -.
DR   KEGG; bab:bbp_422; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_023843_1_1_6; -.
DR   OMA; RMISIAP; -.
DR   OrthoDB; 1201303at2; -.
DR   Proteomes; UP000000601; 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   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   Pfam; PF13145; Rotamase_2; 1.
DR   SUPFAM; SSF109998; SSF109998; 1.
PE   5: Uncertain;
KW   Cell membrane; Chaperone; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..511
FT                   /note="Putative chaperone PpiD"
FT                   /id="PRO_0000193422"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0ADY1"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..511
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P0ADY1"
FT   DOMAIN          227..281
FT                   /note="PpiC; truncated"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   511 AA;  61944 MW;  86CE85DD9A50A905 CRC64;
     MHKLTSKLSN LILLLLIIII FISLILTNFN NYLLENLSEY EIKINNTEIS REEFIQRYNL
     ECFYNDKNFK NDIITNPKNP KYISEIYNIT LSNIIYESLL QQYVHQLHFN IDYSHVKNYI
     YKQTIFRQNQ KFNKEKYYEY LKKLQISSNE YIKKVMTYLE IKEFIKTLTN TDFILNNEKN
     NILKLFEQGR IVNKSYVNLN NLKLIEHISN KELKRYYINH KHQFLSPKKF KISYFLINKN
     NVFVPCIKKF YFKNKDNTFQ HELFLQHKKS KKQNDNIIKK LLTTHTNTSQ FKNIIQKNNI
     CIHHTPWLTQ TLYKHEKLPK KLLKYIINNN ILFHNNKNTI KNYPTIIHMN NNNAYVLWIQ
     KYEKATIENF SKKIRKKIIN ILKNEHSKKI RYQIVQKIVY QLNHGDTNLF SQLKLKFSNS
     EYYSRFNTNT LTNKIFSLPI PKKGQKIYFI FHDQKKLFLY QFSNIFYFKL TKKQKKMIAS
     YISQSHSEII LNAILENLYK TAHISYKGYI N