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Database: UniProt
Entry: A0A1W1Y0K4_9CLOT
LinkDB: A0A1W1Y0K4_9CLOT
Original site: A0A1W1Y0K4_9CLOT 
ID   A0A1W1Y0K4_9CLOT        Unreviewed;       247 AA.
AC   A0A1W1Y0K4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN   ORFNames=SAMN02745134_03849 {ECO:0000313|EMBL:SMC29321.1};
OS   Clostridium acidisoli DSM 12555.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121291 {ECO:0000313|EMBL:SMC29321.1, ECO:0000313|Proteomes:UP000192468};
RN   [1] {ECO:0000313|EMBL:SMC29321.1, ECO:0000313|Proteomes:UP000192468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12555 {ECO:0000313|EMBL:SMC29321.1,
RC   ECO:0000313|Proteomes:UP000192468};
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; FWXH01000041; SMC29321.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1Y0K4; -.
DR   STRING; 1121291.SAMN02745134_03849; -.
DR   OrthoDB; 14196at2; -.
DR   Proteomes; UP000192468; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.1040; -; 1.
DR   Gene3D; 3.10.50.40; -; 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; PTHR47245:SF1; FOLDASE PROTEIN PRSA; 1.
DR   PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR   Pfam; PF13616; Rotamase_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   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW   ProRule:PRU00278}; Reference proteome {ECO:0000313|Proteomes:UP000192468};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          113..202
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   247 AA;  28450 MW;  86AD2E3E379B0BD5 CRC64;
     MKNKILAIVN GKEITENDIQ QSISRFPEDR RQYLSTEQGK KQLLEQIISF ELIYNEAKDN
     GLENDAEYKD QIEAMKRELL TQLAIKRILD EAKVSEDDAE KYYEANKAVF KEAGKVNAKH
     ILVDTEDKAL KIKKEIQEGK SFEDAAREYS TCPSKAQGGD LGSFTRGQMV PEFEDVAFSQ
     EVGIVGDPVK TQFGYHIIKV ESRKEEEPKA YEEVKEAIIN RLTQERQNMK YTEHTENLKK
     KYSVDIK
//
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