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Database: UniProt
Entry: A0A1B6Y8D6_9BACT
LinkDB: A0A1B6Y8D6_9BACT
Original site: A0A1B6Y8D6_9BACT 
ID   A0A1B6Y8D6_9BACT        Unreviewed;       591 AA.
AC   A0A1B6Y8D6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-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=A8B79_07590 {ECO:0000313|EMBL:OAN61314.1};
OS   Balneola sp. EhC07.
OC   Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Balneola.
OX   NCBI_TaxID=1849360 {ECO:0000313|EMBL:OAN61314.1, ECO:0000313|Proteomes:UP000078514};
RN   [1] {ECO:0000313|EMBL:OAN61314.1, ECO:0000313|Proteomes:UP000078514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EhC08 {ECO:0000313|EMBL:OAN61314.1,
RC   ECO:0000313|Proteomes:UP000078514};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAN61314.1}.
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DR   EMBL; LXYG01000017; OAN61314.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B6Y8D6; -.
DR   STRING; 1849360.A8B79_07590; -.
DR   InParanoid; A0A1B6Y8D6; -.
DR   OrthoDB; 9812372at2; -.
DR   Proteomes; UP000078514; Unassembled WGS sequence.
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; -; 2.
DR   Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 3.
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; PF13145; Rotamase_2; 1.
DR   Pfam; PF13623; SurA_N_2; 1.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078514};
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..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          452..550
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|Pfam:PF13145"
SQ   SEQUENCE   591 AA;  66316 MW;  8BF486DA13D71DD0 CRC64;
     MGLMETLRNG TKYIVIILIV SFGLIWVLAD VDFFGAMQAG PNNLGQVNGD DISLQEYNQR
     VQYYNNLYVQ QTGNSMTPEI TAIYEQQVWD ELVNSRLIEQ KMDELGITVT DAELLDMVYG
     DNPDPIIVQN FSRADGTIDR AAIDQVLTNT EFSQQAISLD LQLRQKRRQE KLTNYIAAGV
     QVTNEQVEQE YLKQNTFADL SYVRFPFADI SDEEISVTDA DLKDYYNANK EQYKREENYR
     ASVVKFSYLP TADDTAAIFK EVTDLRSSFA EAESDSLFLN RRQSTTPYSA TFIDKDDVRE
     EYSAVLDIEE GEVTEPFLNA GQVSIIKNVE ENGNEIKFVV FSKQIEALQG TIRDANEEAR
     EFQYYADEET DFASEAERVD TEIQSIFATK GSSFISGLGN SQQVLTFLER ADEGDISNVI
     ELGTDFVVVQ LDEKTKEGYR SLEDVKAQIQ TQVKLEKKKA LAVENAKQAL ASNPTVEALA
     AATEKEIITA EGLAESSAVL TRAGREPKVI GAIFELEEGE TSGVIEGNSA AYIVNVTSKQ
     TPSIDNLDEA TRQQIRTRLE GEINQKFGAI WLEQLKKEAE IVDNRSRLIQ S
//
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