ID A0A2S4MFR5_9BURK Unreviewed; 647 AA.
AC A0A2S4MFR5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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=B0G62_10347 {ECO:0000313|EMBL:POR53475.1};
OS Paraburkholderia eburnea.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1189126 {ECO:0000313|EMBL:POR53475.1, ECO:0000313|Proteomes:UP000237381};
RN [1] {ECO:0000313|EMBL:POR53475.1, ECO:0000313|Proteomes:UP000237381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 18070 {ECO:0000313|EMBL:POR53475.1,
RC ECO:0000313|Proteomes:UP000237381};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JAN-2018) 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:POR53475.1}.
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DR EMBL; PQGA01000003; POR53475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4MFR5; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000237381; 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:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 6.10.140.970; -; 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; IPR023058; PPIase_PpiC_CS.
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; PF13624; SurA_N_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 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 ECO:0000313|EMBL:POR53475.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000237381};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 269..374
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 647 AA; 69843 MW; C6DA578E6113F43C CRC64;
MLDFFRNHKR LMMLMLMLVI LPGLGFVGIQ GFRGFFDESA NVASVNGHKI TRVDYDSAAR
QQMDQARQMM GAQFDASMFD TPQHRKDILD GLIQQRVLAD EVQRLHLTAS DEAVRRTLLA
DPIISSLKNP DGSIDLDKYK QLLAMQGMTP EQYDERVRYS LAMQQLPAAL VNSAFTPKAL
AQQLTGLSEQ QREVQGLAFH ASDYASKVQP TDAQMQAYYD AHKNEFATPA TAQIQYLVLS
AATVAATVNP SDADLKKYYD DNIAHYKSQE EVRASHILIT VAKDASAADR AAAKQKAEQI
LADVKAHPDQ FAQLAQKDSQ DPGSAAKGGD LGYFGPGMIA GGQAFDDAVF KLKKDEISDV
IQSDFGYHIV KVTDIKPSVT KPFDDVKGQI LNDVKTQQAA KVLADTTEGF TSTVYEQAKS
LQPAADKYKL TIQTATVTPK PNPALPPDSP LNNQKFLDAV FANDSVNSHN NTQAIEVGNS
TLISAHVTNF QPAAVPAFAA VKDAVRQKVV AQQAAEMARK DGAAKLADLQ KSKSTDGFSS
ALKVSRGDAQ GLPPSALSAV FKADAQKLPA YVGVDLGNDG YAIYRVNSVT NGPAADGQRL
AAAQQQLAGV GGQSQTQAYL DALRDRSKVK YYGTLGSSSQ QSDGDGQ
//