ID   A0A1Q3RR50_9FIRM        Unreviewed;       466 AA.
AC   A0A1Q3RR50;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=PpiC domain-containing protein {ECO:0000259|PROSITE:PS50198};
GN   ORFNames=BGO41_04300 {ECO:0000313|EMBL:OJV66649.1};
OS   Clostridiales bacterium 38-18.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1895746 {ECO:0000313|EMBL:OJV66649.1, ECO:0000313|Proteomes:UP000185881};
RN   [1] {ECO:0000313|EMBL:OJV66649.1, ECO:0000313|Proteomes:UP000185881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=38-18 {ECO:0000313|EMBL:OJV66649.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJV66649.1}.
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; MKTL01000001; OJV66649.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3RR50; -.
DR   STRING; 1895746.BGO41_04300; -.
DR   Proteomes; UP000185881; 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; PEPTIDYLPROLYL ISOMERASE; 1.
DR   PANTHER; PTHR47245:SF2; SLR0208 PROTEIN; 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; 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}; Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..466
FT                   /note="PpiC domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039605469"
FT   DOMAIN          318..422
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   466 AA;  52356 MW;  14A52978554AA48A CRC64;
     MKGTTDMKKT IAILLSLLMV FGLAACSKSD TNTGDNSFYV YSKDYGFTKN EMAYLYNYVY
     SQSASYLSYL GVDTTKSLKD QEYMDGTSWF DYMMEQAVSY AKDFLIFSET AKDRGIELDE
     SDMNQIQEEL DAVQKSAKEA GFDTVDAFFN DTFGASMTID EYKSFLEKST LAYKVYSEIE
     NSYQFTEDEI KEHYTNNQSE FNYIDYLVYS FAEDADKGIT AEAAEKSADE LAAVTTPEAF
     KAYVENYING INADGALDVE AELAKIDATD MFYTQGDEVS EWGFAADAAV NKTLVTRNTE
     NHVYTVYLLT KLPYRHEAAT VNVRHILVTA DTYGSDDAAK AFAEKVLDEW KAGDATAESF
     GELAKQYTED TGSSATGGLY ENVAEGDMVQ AFNDWIFDPA RVVGDTGIVQ TDYGYHIMYF
     EGKGFDQWQN EVISSMKQVA YSADYSELQK KYPVTVETEK LNEIVE
//