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Database: UniProt
Entry: A0A1G1F723_9BACT
LinkDB: A0A1G1F723_9BACT
Original site: A0A1G1F723_9BACT 
ID   A0A1G1F723_9BACT        Unreviewed;       313 AA.
AC   A0A1G1F723;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=PpiC domain-containing protein {ECO:0000259|PROSITE:PS50198};
GN   ORFNames=A2X56_02325 {ECO:0000313|EMBL:OGW27591.1};
OS   Nitrospirae bacterium GWC2_57_13.
OC   Bacteria; Nitrospirota.
OX   NCBI_TaxID=1801697 {ECO:0000313|EMBL:OGW27591.1, ECO:0000313|Proteomes:UP000177780};
RN   [1] {ECO:0000313|EMBL:OGW27591.1, ECO:0000313|Proteomes:UP000177780}
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:OGW27591.1}.
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DR   EMBL; MHDZ01000070; OGW27591.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1F723; -.
DR   STRING; 1801697.A2X56_02325; -.
DR   Proteomes; UP000177780; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
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; IPR015391; SurA_N.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   PANTHER; PTHR47637; CHAPERONE SURA; 1.
DR   PANTHER; PTHR47637:SF1; CHAPERONE SURA; 1.
DR   Pfam; PF00639; Rotamase; 1.
DR   Pfam; PF09312; SurA_N; 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   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..313
FT                   /note="PpiC domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009573905"
FT   DOMAIN          167..268
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   COILED          37..64
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   313 AA;  35181 MW;  8155C4F6DEA72455 CRC64;
     MKQNLITLIT LPLLLLAHAL TGTADGSVVI DRVVAVVNEE IITMSDLERE VREAQQKDAA
     VNNSMMLEEL INRKLQLSAA KRAGLDATDK EVADAIEDIK RRNSWNTKQF EAALAAEGLT
     VEQYRSELKE NITISRIRDK SVRAGLSVDE AEVRRYYELN SGAYALPQEI RVRQIFIRLP
     ENAPAAEIRV IEEKATRIAA RAKSGENFVA LVKELSEGPS ARLEGDLGYI QRDHALPEID
     LATRALQPGG IAGPLRTNSG FHIIRLEDVR TPVKPLDQVR EEIANSLYQQ KMENNYRVWL
     QTLRNESHVE NRL
//
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