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Database: UniProt
Entry: A0A1W1V0F1_DESTI
LinkDB: A0A1W1V0F1_DESTI
Original site: A0A1W1V0F1_DESTI 
ID   A0A1W1V0F1_DESTI        Unreviewed;       350 AA.
AC   A0A1W1V0F1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN   ORFNames=SAMN00017405_1165 {ECO:0000313|EMBL:SMB86484.1};
OS   Desulfonispora thiosulfatigenes DSM 11270.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulfonispora.
OX   NCBI_TaxID=656914 {ECO:0000313|EMBL:SMB86484.1, ECO:0000313|Proteomes:UP000192731};
RN   [1] {ECO:0000313|EMBL:SMB86484.1, ECO:0000313|Proteomes:UP000192731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11270 {ECO:0000313|EMBL:SMB86484.1,
RC   ECO:0000313|Proteomes:UP000192731};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00000971};
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DR   EMBL; FWWT01000013; SMB86484.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1V0F1; -.
DR   STRING; 656914.SAMN00017405_1165; -.
DR   OrthoDB; 14196at2; -.
DR   Proteomes; UP000192731; Unassembled WGS sequence.
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; IPR027304; Trigger_fact/SurA_dom_sf.
DR   PANTHER; PTHR47245:SF2; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE HP_0175-RELATED; 1.
DR   PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR   Pfam; PF00639; Rotamase; 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; PS50198; PPIC_PPIASE_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW   ProRule:PRU00278}; Reference proteome {ECO:0000313|Proteomes:UP000192731};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..350
FT                   /note="peptidylprolyl isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038589477"
FT   DOMAIN          169..261
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   REGION          305..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          178..209
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   350 AA;  40231 MW;  FA2FB24C2248F9D2 CRC64;
     MKRFASILLL GVLIFSLTGC QSKDYVAKVN DEVITRDELD NKVVQIAASE GLNLEDPQYA
     SFKDYFDLQV LNQIIDEKLL MKQAEKKNIK ADSKVVDEKL AQIKGQFASD KEYKEYYEKQ
     FKMSEKEIKQ VVTDSIIMEK LFAEITKDVK ITTDLQTYYN ENKEEFNQPE KIKAKHILVE
     TEKEAKEILK QVTENKADME KLAQEKSIDP SAKENKGNLG YFPRGSMVPE FEEVAFALNA
     GEIAKEPVKS QFGYHIIQVE DKVAAKQLSF EEAKGQIEDK LLTGAKNNKV MEYLTEVRKE
     AKIENKLEKE VNEKLEEEKK TQTNQPVDET KSDDTKADDK VKDKEPEEKK
//
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