ID   PPID_HAEDU              Reviewed;         620 AA.
AC   Q7VKX4;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Periplasmic chaperone PpiD {ECO:0000250|UniProtKB:P0ADY1};
DE   AltName: Full=Periplasmic folding chaperone {ECO:0000250|UniProtKB:P0ADY1};
GN   Name=ppiD; OrderedLocusNames=HD_1737;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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; AE017143; AAP96493.1; -; Genomic_DNA.
DR   RefSeq; WP_010945522.1; NC_002940.2.
DR   AlphaFoldDB; Q7VKX4; -.
DR   SMR; Q7VKX4; -.
DR   STRING; 233412.HD_1737; -.
DR   EnsemblBacteria; AAP96493; AAP96493; HD_1737.
DR   KEGG; hdu:HD_1737; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_023843_1_1_6; -.
DR   OMA; DNSQGWI; -.
DR   Proteomes; UP000001022; 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;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..620
FT                   /note="Periplasmic chaperone PpiD"
FT                   /id="PRO_0000193425"
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..620
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   620 AA;  69557 MW;  8424E9448591D6EA CRC64;
     MIEKMHERTN SVAFKVIFAL VSLSFVLTGI GTGLVGADTS AVKVNGTTID QHAFNTAKAR
     QQNVLNAQLG ERFWDLLDTP EYAKQFNQSV LDGLVNDELM RQYAKDLKLG ISANQIKSQI
     VNSQIFQQDG KFNNELYQHT LRNNGLTADG YAAIVNEGML LSQIQKGIVE SDFSVPVTEA
     LLAKLLLQQR QVRLATYPIA KEIANQTASV EELQKYYDAK KTDLVEPEQL VVEYVTFMPK
     DIEKNIQVTD EQVATYYEKN KADFVTKGET HLAHIQLANE EKAKQVAEAL KQGTDFAMLA
     NDTSTDSLSA QQGGDLGWTK AGIFPEIFEQ TANALAINEV SEPVKVDNNY HIIKVLDRKE
     DVALPFEMVK DKIVKIIRDE LLLTEYSNIS HEMANKAFEN SSSLAEVAQI AGVNVQTSTQ
     FNREHIPADL NNEKVIKALF NGELRQSGQN SDALDVGNER EPKTMFVRVR DFYPERVRTF
     DEAKADIEQI VKHQKAEQLL LAKAEENVKA LNEGNAVNVD FNEAETLVYA KRADNPILFK
     TVFAMQKPTD KPTYQVTHNQ QGDVVIVSLE KVIDGKQEEF APLASQLKQL DQTLLRNDLL
     KDLRSRASVD VNQNFIEQLK