ID A0A3A9UWT4_9FLAO Unreviewed; 708 AA.
AC A0A3A9UWT4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=D1817_14230 {ECO:0000313|EMBL:AXT20983.1};
OS Flavobacteriaceae bacterium.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1871037 {ECO:0000313|EMBL:AXT20983.1, ECO:0000313|Proteomes:UP000260281};
RN [1] {ECO:0000313|EMBL:AXT20983.1, ECO:0000313|Proteomes:UP000260281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU392 {ECO:0000313|EMBL:AXT20983.1,
RC ECO:0000313|Proteomes:UP000260281};
RA Song W., Thomas T., Edwards R.;
RT "Complete genome sequences of pooled genomic DNA from 10 marine bacteria
RT using PacBio sequencing.";
RL Submitted (AUG-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}.
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DR EMBL; CP031964; AXT20983.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9UWT4; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000260281; Chromosome.
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; PF13145; Rotamase_2; 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:AXT20983.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000260281};
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..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 346..454
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 708 AA; 78625 MW; 69B2F3D291243D9D CRC64;
MAILNKIRQQ SLVLILVIAL ALFAFILSGL FDGSTNFSSK SQNIVATVNG TDIGREEFMS
KVENAQRQFR GGSTSQAMNF VWDQELRRVI LQEQYDALGI SVERDQMRSL LERNLGTFPE
FQNEAGLFDE GKLNEFIANL KEISPEQGFL NGSPINYQTW VELYESQIAT RGIEESYFNM
IRAGLTGTLT EGELDHKLTN DNVDVNFVQI PYVLIPDSTI TVTRSDITKY INDNPSKYEI
ENSRDLSYVV FRETASLEDE NAIKQSLITS LDNKDGRVGF KNTEDNAGFL ISEESAIQYN
DNFQYKNQLG IASDSLFNLQ KGDTYGPYRE GNMFKITKVV EARQLPDSVK VRHILIPFVP
GNGQDPATVK TEDQAKTTAD SILTILKRNR SKFNDLLELS SDLIPGKNTN GEIELAYNSG
IVGPEMSKFS FENKRGDLEV VKTTYGFHIT EILEQKNQQK VLKVATLAKR IDPSEETIDE
VFKATSKFEI AVANKDFNDE AEANKYTVRP VNGIKELDEN IPGIGIQRAM VRWSFEKETE
VGDIKRFNIP GGGYAIAILN AKKPKGLMSV ENASITAIPE IRKQKKAEII KNRIVAGTME
QIAAAEGQTV KTALALNMKN TTLTGAGFEP KVIGTAFGLE EGETSQLIDG NSGVFIVQVT
KITPAAELPN YQAAANRIGV AKSNQSVTAL YEALKKAADI EDNRATFY
//
