ID A0A0F7JX73_9GAMM Unreviewed; 638 AA.
AC A0A0F7JX73;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=AAY24_07555 {ECO:0000313|EMBL:AKH20227.1};
OS Sedimenticola thiotaurini.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Sedimenticola.
OX NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH20227.1, ECO:0000313|Proteomes:UP000034410};
RN [1] {ECO:0000313|EMBL:AKH20227.1, ECO:0000313|Proteomes:UP000034410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH20227.1,
RC ECO:0000313|Proteomes:UP000034410};
RX PubMed=26089430;
RA Flood B.E., Jones D.S., Bailey J.V.;
RT "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, a
RT Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-Oxidizing
RT Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL Genome Announc. 3:e00671-15(2015).
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; CP011412; AKH20227.1; -; Genomic_DNA.
DR RefSeq; WP_046859163.1; NZ_CP011412.1.
DR AlphaFoldDB; A0A0F7JX73; -.
DR KEGG; seds:AAY24_07555; -.
DR PATRIC; fig|1543721.4.peg.1568; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000034410; 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 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000034410};
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 265..367
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 638 AA; 71045 MW; A5B007C4D039D31D CRC64;
MLQSIRERAQ GVIAWFIVIL ISVPFALFGI NSYLGGGSEP VAATVNGQEI TQREFDNGYR
DFRENLRQRL GDDYRPEMID EKKLRQDVLQ MMIRNSLLLQ KSDELGLRVG DDLVKQVIVS
IPAFRVDGRF NQEAFERALR LQGQTQAGFV EQVRRGLVSE QLSKAVSDSE FTTKSEMTSL
VKLRLQRRDF EYLVLPAENF LENVEVSDQS VEAYYAAHQD EFMAPERVKI SYLDLDIDSI
AKTLTSTEED LQAYYEQHQS LYKTAEQRRA SHILIAVDEG SDQATIDQAQ SLAQAALERV
RNGEDFAAVA KELSQDPGSA DQGGDLGFFE TGVMESAFDE VVFKLKPGEV SDLVRTPFGF
HIIKLTDIRE PAGKSFAEAK DEVKKAYLKS EAERLFYEYA ERLGNIAYEE PHSLQPAADD
LGMELKESDW ITRNGGEGML GAPKVIAAAF SDDVLVSGNN SEAIELNPEH VLVLRVLEHE
EAAVKTLDQV KQSIVDKLRL EKAMELATQQ GAEWVNRLSQ GETLATVAAD KGAQLNPRKV
VSRDEQDIPA DLLGHLFMMP HPTGDQPVYG QLALSNGDLA LIALHKVIDG SLEEAAEVGG
EDVLNRVMTE SRGKSYFQHL QNNLRASADV VITDQATE
//
