ID A0A1W9RRS6_9BACT Unreviewed; 475 AA.
AC A0A1W9RRS6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=B6D55_03915 {ECO:0000313|EMBL:OQX87268.1};
OS Candidatus Omnitrophica bacterium 4484_70.2.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1970783 {ECO:0000313|EMBL:OQX87268.1, ECO:0000313|Proteomes:UP000192395};
RN [1] {ECO:0000313|Proteomes:UP000192395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (MAR-2017) 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:OQX87268.1}.
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DR EMBL; NATM01000028; OQX87268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9RRS6; -.
DR STRING; 1970783.B6D55_03915; -.
DR Proteomes; UP000192395; 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; -; 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; PF13145; Rotamase_2; 2.
DR Pfam; PF13624; SurA_N_3; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 207..330
FT /note="PpiC"
FT /evidence="ECO:0000259|Pfam:PF13145"
FT DOMAIN 342..438
FT /note="PpiC"
FT /evidence="ECO:0000259|Pfam:PF13145"
FT COILED 196..223
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 475 AA; 56898 MW; C1DD734343378AF6 CRC64;
MLTKFRRRHI KRILWGIVIF VVPAFVFWGS SFLRRRQKNG QNIVGKIANH NVTYSQFLEY
RTMAQISLQL LLGEDFYRKL SFKDRNKEIE RRAWEYALLL WKAKKEKIKV SDKEVAEEIK
KRFFPKGKFD KRLYFIFVRR ILRIEPYIFE RYLRKIIKAE KVLNKYLKVE VSDQEVKETY
KKYNEKAKIA YIPIPYKKFD AEIKLKEEEI KNFYEKNKEL FKEGAKAKIK YILLKENDKK
EIEKSFKNLT KIKNIEIIGK KFNLPIKTTG FIGINDTIEG IGEEKKINYV ALSMKTGEIG
PLLKLKNGYI LFQKIEEKPA SISPFSTARE KVEAILRRQK REAKAKEFAR NILEEIKRKN
IKNLKDIAEE YKLEVKETDF VKYYDPILKE IGPNEDLSKI VFHLKKGEIW SSPFISSQKI
YIIQLTDFIP IEKEKFKKEK EKYKQRLFVQ RALLKRLKFF SQLEKEANLV IYTQL
//
