ID A0A372K715_9BURK Unreviewed; 644 AA.
AC A0A372K715;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=D0B32_09395 {ECO:0000313|EMBL:RFU47754.1};
OS Paraburkholderia sp. DHOC27.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2303330 {ECO:0000313|EMBL:RFU47754.1, ECO:0000313|Proteomes:UP000263097};
RN [1] {ECO:0000313|EMBL:RFU47754.1, ECO:0000313|Proteomes:UP000263097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHOC27 {ECO:0000313|EMBL:RFU47754.1,
RC ECO:0000313|Proteomes:UP000263097};
RA Gao Z.-H., Qiu L.-H.;
RT "Paraburkholderia sp. DHOC27, isolated from subtropical forest soil.";
RL Submitted (AUG-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:RFU47754.1}.
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DR EMBL; QVQV01000002; RFU47754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372K715; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000263097; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PF13624; SurA_N_3; 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 ECO:0000313|EMBL:RFU47754.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000263097};
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..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 269..374
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 644 AA; 69662 MW; 6CDABEEA04AB9E11 CRC64;
MLDFFRNHKR LMMFMLILVI VPGLGFVGIQ GFRGFFDESA NVASVNGHKI TRVAYDDAMR
QQLDRARQML GAQFDMKSFD TPERRKEMLD GLIEQRVLAD ETQRLHLTAS DDAVRRTLLS
DPVISSLKNP DGSIDVNRYK ELLAMQGMTP DQYDERVRYT LATQQLPGSI EGSAFTSKTL
AQHLTDLSEQ QREVQSLAFN PHDYASKVQP TDAQLQAYYD AHRNDFATPA TASIQYLVLS
PATLAAAIQP GDADLKKYYD ENIAHYQTAP QMRASLILVS VAPNASAADK TAAKQKADAL
LAQVKAHPDD FGKIAEQSSQ DPASASKGGD LGYFGPKMMA GGPAFDDAAF KLKKDEISDV
VTTDVGYLIL KATDVKPSVT QPFDTVKDAI AKDLTAQMAA KQFSDDSDGF TSLVYEKAKS
LQPAADKYKL QIQTATVTPQ PNTGLPPTSP LNNPKFLSAV FANDSAQARN NTQAIDVGSN
TLIAAHVTDF KPAAVPPLDV VKDAVRQKVI AVQADEMAHK DGVAKLAELQ KSNATTGFAA
PVKVSRNDAQ GLPPAALSAI YKANGQKLPA YVGVDLGDDG YAIYRVNAVL PGAPIDPQRL
TAAQQQIAQV EAQSEMTAYI DALRARSKVK FYGSLDAGQP GGDQ
//