ID A0A365P1M0_9FLAO Unreviewed; 700 AA.
AC A0A365P1M0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-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=DPN68_06815 {ECO:0000313|EMBL:RBA28417.1};
OS Flavobacterium tibetense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2233533 {ECO:0000313|EMBL:RBA28417.1, ECO:0000313|Proteomes:UP000253319};
RN [1] {ECO:0000313|EMBL:RBA28417.1, ECO:0000313|Proteomes:UP000253319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YH5 {ECO:0000313|EMBL:RBA28417.1,
RC ECO:0000313|Proteomes:UP000253319};
RA Xing P., Phurbu D., Lu H.;
RT "Flavobacterium tibetense sp. nov., isolated from a wetland YonghuCo on
RT Tibetan Plateau.";
RL Submitted (JUN-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:RBA28417.1}.
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DR EMBL; QLST01000007; RBA28417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365P1M0; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000253319; 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 ECO:0000313|EMBL:RBA28417.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000253319};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 346..451
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 700 AA; 77136 MW; 15B9D21DAC78FFDF CRC64;
MAVLSKIRQR SFVLIVIIAL ALFSFVLADV IQSGGFGSNS NNVGSVNGTD ISSIEFMQKV
AQVEKQGQNT SNTQAINSVW EQHVRSIIIG DEIEKLGLGI AGDQLVKVIK ENPYFAQNPQ
FLNAAGTFDE NKFREFVKSI KNDPNQDRWR EWQNFEAEVE KTAIEQLYYN LIKGGVYTTK
AEGKFKHMVE NKKANFEYVT VPYSSINDEE VKVSDDEIIA YMKKNAKKYK SDNTRSIEYV
LIENKPSDED EKAMVGAINS VLYGKVVYNE KTQQNDTLPA FKDVTDVASF VNANSDIKFD
STYLAKSQLP VEYQEQLFNL SKDEVFGPYT YSGFQCVSKM IDKKANASAK ASHILISYEG
AERSSATRTK DEAQKLANEL LAKAKANPVG FGLLADENTD DPGSKGKGGE YDNIMPGQMV
PKFNDFVFDS PVGAIGLVET EFGFHVIKVA DKYSSVLIGT VAQKIEPSSK TIDAVYTTAS
KLEADATTKN FEEIAKAANL TVVPAGNIKA FDEFVSGLGA QREVVRWTFN EDTNVGSVKR
FETPQGYIVA KLKEKNDTGL LPLEYARENV GVILRNEKKA DLIKKKMTGA TLEEVAKATG
SSVLTANDVI LGNVLIPNVG QEPKVVGTAF ALATGKTSKL IDGNSGVFII RAKSVIEAPA
VNAYTSQITQ EMQTQQNNAQ MRAYEALKDK ATIKDNRFQF
//
