ID   A0A142L6R7_9BACT        Unreviewed;       703 AA.
AC   A0A142L6R7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE   AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN   ORFNames=AEM51_13730 {ECO:0000313|EMBL:AMS27913.1};
OS   Bacteroidetes bacterium UKL13-3.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1690483 {ECO:0000313|EMBL:AMS27913.1, ECO:0000313|Proteomes:UP000075224};
RN   [1] {ECO:0000313|Proteomes:UP000075224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Driscoll C.B.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004382}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004382}; Periplasmic side
CC       {ECO:0000256|ARBA:ARBA00004382}.
CC   -!- SIMILARITY: Belongs to the PpiD chaperone family.
CC       {ECO:0000256|ARBA:ARBA00038408}.
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DR   EMBL; CP012155; AMS27913.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A142L6R7; -.
DR   STRING; 1690483.AEM51_13730; -.
DR   KEGG; bbau:AEM51_13730; -.
DR   Proteomes; UP000075224; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
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; PF13616; Rotamase_3; 1.
DR   Pfam; PF13623; SurA_N_2; 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 {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075224};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          350..444
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   703 AA;  78040 MW;  CCF959738976597D CRC64;
     MSVLEKIRNK SGLAIVVVGG ALALFVISDA LQSNSRLFGG NDTTVGEIDG ESISVQQFEQ
     EFQKNLESYK LRSQQPTVDQ NTSDMIREQT WNQLIMDGIM VKQYKELGIG VTNEELFELV
     QGVDPHPQIK SAPIFQNPQT GQYDRSLVVR FLKNMTESND EQAKTSWLEF ENGLAKETES
     KKYNTLFKKG VYATSLEAKS VYNNRNHTTD MDLVAVNFFS VADSTIKVDD SDLKSYFNKN
     KDKYKEKLNT RKLEFVTFDV IPTSEDSANI QKWVADQVTQ FAAATNDTLY VDVNSDSKFD
     TVAHPLSYYP ADVQGAIFTQ PVGGMIGPVF ADGKFKIYKV AGIKEDSLFQ MRASHILFKV
     ENNDTAASLK KAQEIMAEIR KGADFGEKAA QYGTDGTASR GGDLGWFAEG QMVKEFNDYV
     KRGNKGDMGI VKTQFGIHIV KITENKSKKT VCAGVLERAI EPSERTVNGA YNMASQFAAA
     SQGGAENFET AVKEKGLSKR VADNLRENDK TLAGLPDARE VVRWAYNAKV GDVSEVFSLG
     DKYIVGVLSQ IKEKDNANFD DVKERVTADY RKEKKAEQLM ESVKTAMTGA ATLQDVATKL
     QVAVTPVVGQ TFENSNVAYV GPDNAFIGTI FGTKTTGKMV GPIKGDNAIY VANIIRFSEG
     PQTPDYVPYK SEIMSQLAQR VEYGSFEVLK EMKNVKDNRY KFY
//