ID A0A1H8QYE0_9GAMM Unreviewed; 639 AA.
AC A0A1H8QYE0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=SAMN04488052_101859 {ECO:0000313|EMBL:SEO59027.1};
OS Aquisalimonas asiatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Aquisalimonas.
OX NCBI_TaxID=406100 {ECO:0000313|EMBL:SEO59027.1, ECO:0000313|Proteomes:UP000199657};
RN [1] {ECO:0000313|EMBL:SEO59027.1, ECO:0000313|Proteomes:UP000199657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6291 {ECO:0000313|EMBL:SEO59027.1,
RC ECO:0000313|Proteomes:UP000199657};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FOEG01000001; SEO59027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8QYE0; -.
DR STRING; 406100.SAMN04488052_101859; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000199657; 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 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; IPR023058; PPIase_PpiC_CS.
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; PF13624; SurA_N_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 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:SEO59027.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000199657};
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..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 267..369
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 639 AA; 72638 MW; FEE4D8B0059CBF7E CRC64;
MLQSIRDRAT GWIAWVVIIL IGSAFALFGL SNYMEPGGTP RAVATVNGSD ISRDEVGRAY
RNQRQQIEQA YGDDLEITDE IDRQIRRDAL ERLINQRLVA DYIDDRNMTV SDQDLAAIIR
SQEVFHEGGR FSQERYQAVL RANQMNSAQY EQHVRQDALA QQVRAAFTES GLVTEREVDD
LLRLQMQERD VAWLRLDNSA WHDDVEVSDD DIQAYYDEHR DTFVTEERVR LAYVELRRED
LIDGVDVSDE EIETRYEQVR DERYTEDREV EARHILIRVD EDADDDTVSE AQERAEALRQ
RITDGESFAE LAEEYSDDPA SGARGGDLGR VERGDMVEPF EDALFALEEG ELSEPVRSPF
GIHLIEATTS TGGEVTPLDE VRDELRREIA EEQVSNEFFD DLNRLDELAF DSPDTLDDAA
EGLGLEIHET DWITREGGDG IASEPEVLEA AFDREVLEDR MNSAVIELGD DRAVVVRVSE
HEPQEQLELD EVRDEIEARV RDRKAAEAAE AFADEIMERI RAGESPAEIA SEDDRVSFED
IGWVNRQEGG APGQVLRTVF GMVRPENDTP SLERILAAND PVILVLRGVR DGDAEGIDAE
ERRELAERLR ESYGDEAVEQ FLAQLRADAD VEVHDDDYR
//
