ID   PPID_HAEIN              Reviewed;         622 AA.
AC   P44092;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Periplasmic chaperone PpiD {ECO:0000250|UniProtKB:P0ADY1};
DE   AltName: Full=Periplasmic folding chaperone {ECO:0000250|UniProtKB:P0ADY1};
GN   Name=ppiD; OrderedLocusNames=HI_1004;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC22665.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L42023; AAC22665.1; ALT_FRAME; Genomic_DNA.
DR   PIR; B64018; B64018.
DR   RefSeq; NP_439165.2; NC_000907.1.
DR   AlphaFoldDB; P44092; -.
DR   STRING; 71421.HI_1004; -.
DR   DNASU; 950512; -.
DR   EnsemblBacteria; AAC22665; AAC22665; HI_1004.
DR   KEGG; hin:HI_1004; -.
DR   PATRIC; fig|71421.8.peg.1047; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_023843_1_1_6; -.
DR   PhylomeDB; P44092; -.
DR   BioCyc; HINF71421:G1GJ1-1044-MON; -.
DR   Proteomes; UP000000579; 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..622
FT                   /note="Periplasmic chaperone PpiD"
FT                   /id="PRO_0000193426"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0ADY1"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..622
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P0ADY1"
FT   DOMAIN          270..356
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
SQ   SEQUENCE   622 AA;  69590 MW;  EE5900A5381C4EB4 CRC64;
     MLIEKMHNLT NSKISKFILG LIAVSFLVGG MSGYLFSSND TYAAKVNGEV ISQQDFLNRY
     NQEFEIRAQR EGEAFVAQSD SPEFVTALRQ NIVNLMIDQE LLRQYVKELK LGVSDEMIKR
     AIVTDPNFQV KGKFDNAVYQ RILQQNHLTS DGYASILRAS LPLEQIQNGV ANSEFIVPAQ
     VKNSAEVFFQ KRLARLATLS LADEMAKQSV SDDEIKTYYE ANQKSFVQPE QVKVQYIDLS
     ADNISRNLQV TDVEIAQYYQ DNKAQFMTQH LAHIQFANEQ DAKVAYEELQ KGANFADVAK
     AKSLDKISGE NGGDLGWVNE NELPKAFEDA AAALQVGQYS QPINVDGNYH IVLVQERKAQ
     SLENVKAQIA DLVRKSLMES RYFSLEKQAS DKAFEDSKSL NTAAQAAGVK VQESDYFSRQ
     NVPAGLNFPN VIYTIFESDT TNVGMNSEPI NVGDYHTIIV RVLDRKAEGV KSLEEAKIDI
     ETFLKRQKAE NALNGKAQQA VKKLSENPES KVDGINFSSE QTFTLSENKD PILTNGIFSI
     AKPESSKALY QVVHNSNGDV VVVALNKVEQ GSLSEKELSQ FAMQLLRSHQ SELQVQLIQG
     LRERAKIEVN DSFINQDDEA QQ