ID A0A1G0WS52_9BACT Unreviewed; 725 AA.
AC A0A1G0WS52;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, 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=A2475_08620 {ECO:0000313|EMBL:OGV24264.1};
OS Ignavibacteria bacterium RIFOXYC2_FULL_35_21.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798452 {ECO:0000313|EMBL:OGV24264.1, ECO:0000313|Proteomes:UP000177327};
RN [1] {ECO:0000313|EMBL:OGV24264.1, ECO:0000313|Proteomes:UP000177327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV24264.1}.
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DR EMBL; MHAY01000013; OGV24264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0WS52; -.
DR STRING; 1798452.A2475_08620; -.
DR Proteomes; UP000177327; 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; 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; PF13623; SurA_N_2; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 2.
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 366..463
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 725 AA; 81501 MW; 8C80F1100A2AAA13 CRC64;
MGTMERMRKT SPYFLAAFAV LFVGFMVASD ADIGSLIQGR GSIQTELIGK INGEEILYKD
FDLKVKEVIE QKRKQSSDPN ANIDEDQVIN QVWSQMVDET LLKQEAKKAG VIVSDEEILD
VLLDNPPESL RKPFTDSTGT FNNQLYLELV TNPDKMGEAL GPNVSAEEKQ KAIDDFKKYL
IDFEKYLRQQ KLAEGLIAVV SSSVSAVSPQ YAKEKYIYDY TSSDVDFLFF GRDEIQDNQV
QVTEKEIADY YDKHKQAYKQ KPQRRLKYIK FDIVPNIDDT IRAGKKVDRI TADLASVTTI
LEKDSVFDLK MSEFGGNNPE FTLIKDIPDF KLNMLQTMNV NDIIGPVMTP DGITFLRLDG
KRSGENEVVK ASHILLKFSV NKDSTKAEAE RIMARAKGGE DFAELARKYS GDPGSASKGG
DLGFFGKGAM LKPFEEAAFA AAPGSIVGPV ETEYGYHIIK VFEKKSDEIK YSEIVIKPIV
SNTTKNMLFR NAYSFQKQVE EGHSFDNLAE KSKYKVQQTM FFTKGTPVLG SQYLSDLAFE
SETGTVLQPL ELKNQGLFVC VVTDSRENGL RTLKDMKEFI RVQVTNIKKL DAVKSKADAA
YSKVAGLDAL SKASTVDPLL VVKSLAGVQN TGNVQGIGED FVFTTKATNL PVLAISKPFR
GTMGYYIMQV KSRLAPPAES IEKGYMQYIT KMKKDNYQNE FYQWFGKIKQ DADIEDYRVK
FYREY
//
