ID A0A1Q6A671_9SPHI Unreviewed; 705 AA.
AC A0A1Q6A671;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=RG47T_4991 {ECO:0000313|EMBL:OKS89507.1};
OS Mucilaginibacter polytrichastri.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1302689 {ECO:0000313|EMBL:OKS89507.1, ECO:0000313|Proteomes:UP000186720};
RN [1] {ECO:0000313|EMBL:OKS89507.1, ECO:0000313|Proteomes:UP000186720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RG4-7 {ECO:0000313|EMBL:OKS89507.1,
RC ECO:0000313|Proteomes:UP000186720};
RA Li Y.;
RT "Whole Genome Sequencing of Mucilaginibacter polytrichastri RG4-7(T)
RT isolated from the moss sample.";
RL Submitted (NOV-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:OKS89507.1}.
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DR EMBL; MPPL01000001; OKS89507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q6A671; -.
DR STRING; 1302689.RG47T_4991; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000186720; 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 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; PF13623; SurA_N_2; 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000186720};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 349..447
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 705 AA; 76568 MW; BB922C10DA1BDB06 CRC64;
MGLMSFLRNR MGTIVVVIIG LALFAFIAGE VVQYGKSFFT GDQTTVGEIS GEKINYEAFS
ARLDQNTKQY QQQFGQNLTP QLTSYVQNIT WNQYLSQIIF KKEVEKVGVV VGADETKSMI
SGTNPDPEVA RNFTNPQTGQ LDRAQLNQFL NNMQNAPASD PMRAQWADFV AARIDAKKME
KYLAIVHNGL YVNSLEATDD YEAKNKLANF KYVTLPYAAV PDSKVTISDG DYQAYYDEHK
SSFKNPQELR TFKYVSFNAA PSKEDTAAIK LQADKLAADF KASTNDSLFV QINAIDAVNK
AALAFVHKGQ LDPKIDSVMF NAPKGFVYGP YVSNGSYKVS KLVDEQVGPD SVKARHILIN
PATEGGLPKA IAKADSIKKL IEGGKSFGDL AKMYSIDKAS AEKDGELGTF GRGAMVPVFD
DAVFNGKKGD LKVITSQFGV HVIQIEDQKG SSKVVKVATV DRPLLASSKT QSEAFSKAQT
FLSATNGDNF DAQAKKEGLE VKTAPDVTGI AAGLPGLDNA REVVKWVFKA DKGDIADKAF
TVGTQYIVPR VTEIKLEGYL ALDAVKKQIQ PAVLNIVKAK QLTEKLQAAA NGASSIDQVA
QKAGATVVPV ENIVFANPVL PGIAQENKLI GSIFGSQPNK VSKPIAGDHG VYVYVLNSFI
NPAPLTNAVT VKQQLGQAML QRADNQVFDA LKDKANVKDY RAKFL
//
