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Database: UniProt
Entry: A0A0L6U3X0_9FIRM
LinkDB: A0A0L6U3X0_9FIRM
Original site: A0A0L6U3X0_9FIRM 
ID   A0A0L6U3X0_9FIRM        Unreviewed;       497 AA.
AC   A0A0L6U3X0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, 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=AKG39_01805 {ECO:0000313|EMBL:KNZ43211.1};
OS   Acetobacterium bakii.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Acetobacterium.
OX   NCBI_TaxID=52689 {ECO:0000313|EMBL:KNZ43211.1, ECO:0000313|Proteomes:UP000036873};
RN   [1] {ECO:0000313|Proteomes:UP000036873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8239 {ECO:0000313|Proteomes:UP000036873};
RA   Song Y., Hwang S., Cho B.-K.;
RT   "Draft genome sequence of Acetobacterium bakii DSM 8293, a potential
RT   psychrophilic chemical producer through syngas fermentation.";
RL   Submitted (JUL-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:KNZ43211.1}.
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DR   EMBL; LGYO01000006; KNZ43211.1; -; Genomic_DNA.
DR   RefSeq; WP_050738656.1; NZ_UOGO01000001.1.
DR   AlphaFoldDB; A0A0L6U3X0; -.
DR   STRING; 52689.AKG39_01805; -.
DR   PATRIC; fig|52689.4.peg.3064; -.
DR   OrthoDB; 14196at2; -.
DR   Proteomes; UP000036873; 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; PF13145; Rotamase_2; 1.
DR   Pfam; PF13624; SurA_N_3; 2.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 2.
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:UP000036873};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          334..426
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   497 AA;  55406 MW;  55787A8D77BC7EA4 CRC64;
     MKTKKLRTIT LLLAVTILIS FVGSGCSLVK VNPEADKKQV VAEINGEQIL KESYNNYLAY
     YQMYYEASGM TFPTDVELKQ LQLDLLDDLV RVETMAAQGK KDGVTVDEAV LTADAESIIT
     SIKTTLGDEK YAAALAKNNT DTGSFETFMK AFVANNEYAN TVAANYNSAL LLDPAKELTT
     VVGTVGGDNV TKDVYNYRLS NEEFLAYYQN QEALATDDET MKTVNDNIFN TIAEQKAMTK
     YAEENNLTLA QEDVDGYITS QQAFVNSLLP GDETLQQYLD GKYLTVAQYR EFEKQDAKAT
     AAAAAIQADL ASKAKVSDKE IKTYYDENKN SYDTSTVSAK HILATDETLA KQIYEEAKNA
     KTVEEFDAVM TKYQTVEGVS QATDLGAFTY ATMVSAFSDA AFGMEKNTVS EPVKTDYGYH
     IIYVYDKNQA EIPALDTKKE EITEVLKNQK ATEEFDKLKT KLTKKLTIKF DKILTPLETY
     MEQLKTDLNV EVFQNKI
//
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