ID   A0A0M2U4C7_9FIRM        Unreviewed;       323 AA.
AC   A0A0M2U4C7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN   ORFNames=SY88_18285 {ECO:0000313|EMBL:KKM09549.1};
OS   Clostridiales bacterium PH28_bin88.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1605376 {ECO:0000313|EMBL:KKM09549.1, ECO:0000313|Proteomes:UP000034222};
RN   [1] {ECO:0000313|EMBL:KKM09549.1, ECO:0000313|Proteomes:UP000034222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Robbins S., Tyson G.;
RT   "High quality genome sequence of Candidatus Suratobacter aromatica.";
RL   Submitted (MAR-2015) 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};
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:KKM09549.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LAKY01000063; KKM09549.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2U4C7; -.
DR   STRING; 1605376.SY88_18285; -.
DR   Proteomes; UP000034222; 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:SF1; FOLDASE PROTEIN PRSA; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW   ProRule:PRU00278}; Reference proteome {ECO:0000313|Proteomes:UP000034222};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..323
FT                   /note="peptidylprolyl isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039266799"
FT   DOMAIN          175..282
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   323 AA;  36728 MW;  D1FF5BE8C3DE1671 CRC64;
     MKRAKRLIGF LLVLLFPLSA FGCAGSQERQ VVAVVNGEEI LRSQLDHRLE QFKSFLKGQG
     MDVQGKEDSQ AWKEVADQSL ESLIQDVLLR QAAKEQGIDI SREGVEQKIA QVKKMAGSDK
     EFQDFLQQQE LSEEDFSFQI EQGLLAERLY QKVTAEIRVE EQEVQDYFTA NKELLMKAKV
     RQILIPVPPD ENKNNVIEEA KAKSQEVITQ LDNGADFAEV AKKYAEGGLD QTHAGMILEE
     VAVNDPAYPP AFVSAVFSLR EGQHTPEPVR TPLGFHIIRV EEILDSMAEL KGDIERLLLE
     KKKDQAFQKF YEEFRQTAKI QRF
//