ID A0A173MPZ4_9BACT Unreviewed; 701 AA.
AC A0A173MPZ4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=SAMN05421788_1011179 {ECO:0000313|EMBL:SIS78306.1};
OS Filimonas lacunae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Filimonas.
OX NCBI_TaxID=477680 {ECO:0000313|EMBL:SIS78306.1, ECO:0000313|Proteomes:UP000186917};
RN [1] {ECO:0000313|Proteomes:UP000186917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21054 {ECO:0000313|Proteomes:UP000186917};
RA Varghese N., Submissions S.;
RL Submitted (JAN-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}.
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DR EMBL; FTOR01000001; SIS78306.1; -; Genomic_DNA.
DR RefSeq; WP_076376553.1; NZ_FTOR01000001.1.
DR AlphaFoldDB; A0A173MPZ4; -.
DR STRING; 477680.SAMN05421788_1011179; -.
DR KEGG; fln:FLA_5798; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000186917; 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:SIS78306.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000186917};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 339..447
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 701 AA; 75989 MW; 7EA47D34881BB97A CRC64;
MSVIQRIRDK AAWIIFGAIA LALIAFIVQD ASFRRGSLFS NSTTVGKVNG ESIDKKEFDA
KVDLVQQMQG AQNSQRNQLT ASVWNFMVEQ TILHQQLDKL GIVVPGKELS DILFDPTSSP
FAREFTDPQT GVFDVEKAKQ AFAQLKKSRN AEQLNMIMQA YVQPAVDRAL MQKYQALITQ
AVYIPKWMAE KTNADNSAIA NISYVYVPYS TVTDSTVKVS DDEIAAYVSK HPNEFKQEEE
TRSISYVTFD ASANGSDTAA ALNLINELKP EFATTSDAKS FLGTKGTENP YYDGYVTRAN
MKMPNADSIM SLADGQTFGP YLDGSNFTVA KMVGRREMPD SVKVRHILIK EGEQGQLTLP
DSVAKARIDS IEAAVKGGAS FEALVQKYSD DPGSKATNGE YEFASTQFAG LSKEFAEVAF
YGNVGDKKVV KVENGAYAGY HYIEVLSQKN KQIAYKVAYL AKPISASSET IGTASTAAMQ
FASASKSKAQ FDEAANKANK FPSPSPDIKE NDFSIMGLGE NRQFVKWIFE NKVGDVSDPT
EIGDKYVVAI ITGVNKAGTL SARAARPMVE GILKNEKKAQ QILAKFTGNS LEAYAQSTGT
AVQRADSLSF QSPFIPAVGS EPKVVGAAFN KDVQGKVSAA IAGNTGVFAV KGEGVSAKPS
FGGADGQRTA LENSMRSQIG YRALDALRKA AVIKDNRSTF Y
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