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
//