ID G4E3E9_9GAMM Unreviewed; 626 AA.
AC G4E3E9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=ThisiDRAFT_0828 {ECO:0000313|EMBL:EGZ48691.1};
OS Thiorhodospira sibirica ATCC 700588.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thiorhodospira.
OX NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ48691.1};
RN [1] {ECO:0000313|EMBL:EGZ48691.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ48691.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J.,
RA Frigaard N.-U., Bryant D., Woyke T.;
RT "The draft genome of Thiorhodospira sibirica ATCC 700588.";
RL Submitted (SEP-2011) 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:EGZ48691.1}.
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DR EMBL; AGFD01000011; EGZ48691.1; -; Genomic_DNA.
DR RefSeq; WP_006786843.1; NZ_MU255056.1.
DR AlphaFoldDB; G4E3E9; -.
DR STRING; 765914.ThisiDRAFT_0828; -.
DR PATRIC; fig|765914.3.peg.837; -.
DR eggNOG; COG0760; Bacteria.
DR OrthoDB; 9812372at2; -.
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; PF13145; Rotamase_2; 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:EGZ48691.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 265..360
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 626 AA; 70724 MW; 718223C017C86266 CRC64;
MLQKIRDKAT GWFAYIIIIL IAIPFALWGL NEYFGGAGSL VAAEINGTEI PVRAYQQEFQ
QQRRQLAEMF GGRIPAGLID DQQLRDNALQ TLIRRELLAQ LAQERGYGVS PRLVAEEIRA
MEFFHENGQF DSARYQRVLA EQRLNKAQFE ADVRYSLLLL QVEQSLGYAA FLTSADLQEY
ARLREQTRRV SYHTIAAAQF AQQVQIDEAD IERHYQQHGQ RFLRPERLRL AYLMLAPQDL
EAHSEVTEED LRRYYEQHTD RFASPEERRI RHIVLSAQAD DAQAQIQAVR ARIEAGESFA
EVAQAVSQDP VSASRGGDLG FLARGDMDPA LDVVSFTLPQ GVISQPVQIG NTWQLIEVTE
IRAPQREPLE AVRDEIMTDL RSRQVESRYI ELTERLLTES FEQPLSLEPA ADATGLEIAY
TDWMTAQGGE DELATYPEIR RAAFSAEVLQ YQRNSDLIDL PDGRSVVLRV HEHQPSAPRP
LAEVQDEIRA QLADEKMSAL AQQAADEVLQ AIRASTPVSE AFATVPGDAV YSINMRRDTP
DIASTLKQRI FSLPHPETEP QSDVVTLNNG DAVVLVLEQV EDGQVDSAAL ARYRNQLQNV
YANLEAEAVL ESLEQRAKIQ IYRENL
//
