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Database: UniProt
Entry: A0A1F5ADA9_9BACT
LinkDB: A0A1F5ADA9_9BACT
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ID   A0A1F5ADA9_9BACT        Unreviewed;       342 AA.
AC   A0A1F5ADA9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=PpiC domain-containing protein {ECO:0000259|PROSITE:PS50198};
GN   ORFNames=A2Y69_14175 {ECO:0000313|EMBL:OGD16499.1};
OS   Candidatus Aminicenantes bacterium RBG_13_59_9.
OC   Bacteria; Candidatus Aminicenantes.
OX   NCBI_TaxID=1797268 {ECO:0000313|EMBL:OGD16499.1, ECO:0000313|Proteomes:UP000177868};
RN   [1] {ECO:0000313|EMBL:OGD16499.1, ECO:0000313|Proteomes:UP000177868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGD16499.1}.
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DR   EMBL; MEXW01000267; OGD16499.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5ADA9; -.
DR   Proteomes; UP000177868; 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; PTHR47637; CHAPERONE SURA; 1.
DR   PANTHER; PTHR47637:SF1; CHAPERONE SURA; 1.
DR   Pfam; PF13145; Rotamase_2; 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.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278};
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..342
FT                   /note="PpiC domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009516576"
FT   DOMAIN          175..271
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   COILED          89..116
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   342 AA;  39189 MW;  F278412EAA01D44A CRC64;
     MNTKKRTMAF CLAIAARTFL GAGQVVEEIV AIVNDDIITL TEVKAQHEVM IQTLRSQLQG
     EEFEKQYARL KGELVNNMIT DLLLLQAARE KQLNVQEQVK LNIDALKKEN NMESDEDLRR
     ALQGQGMTLE EFTRQMQEQI LKSAIIYSEV DSKIVIDDAE VAQYYRLHPD QFTEPEEYTL
     EAVYLSFEAR SEEEAEARKK EVSEKLKDAD FAALAAEFSD SPMNESKGDL GTFKKGELDK
     TLEEAVSTLK KGETSPWIKA RNGWYLVRMK ERKESRLRSF EEVKQEVMRR IGDERRAKLL
     DEYLKKLKAK SYIKILKPDP FGENLELQAT STAAARAVVH NP
//
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