ID   A0A1Q3GQN5_9BACT        Unreviewed;       457 AA.
AC   A0A1Q3GQN5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Peptidylprolyl isomerase {ECO:0000313|EMBL:OJJ18265.1};
GN   ORFNames=BKI52_25930 {ECO:0000313|EMBL:OJJ18265.1};
OS   marine bacterium AO1-C.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae.
OX   NCBI_TaxID=1905359 {ECO:0000313|EMBL:OJJ18265.1, ECO:0000313|Proteomes:UP000186474};
RN   [1] {ECO:0000313|EMBL:OJJ18265.1, ECO:0000313|Proteomes:UP000186474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AO1-C {ECO:0000313|EMBL:OJJ18265.1};
RA   Buerger P., Wood-Charlson E.M., Weynberg K.D., Willis B., Van Oppen M.J.;
RT   "CRISPR-Cas defence system in Roseofilum reptotaenium: evidence of a
RT   bacteriophage-cyanobacterium arms race in the coral black band disease.";
RL   Submitted (OCT-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:OJJ18265.1}.
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DR   EMBL; MLAY01000009; OJJ18265.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3GQN5; -.
DR   STRING; 1905359.BKI52_25930; -.
DR   Proteomes; UP000186474; 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; -; 2.
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; IPR023058; PPIase_PpiC_CS.
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; 2.
DR   Pfam; PF09312; SurA_N; 1.
DR   SUPFAM; SSF54534; FKBP-like; 2.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 2.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000313|EMBL:OJJ18265.1}; Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186474};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..457
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012162356"
FT   DOMAIN          185..285
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   DOMAIN          288..398
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   457 AA;  51716 MW;  EEFD27BCF3A5BA31 CRC64;
     MQKIMQKSIL KYGLSVAFIL FMVMGSTQSQ AQGGGKLVDK IIAKVNNYII LESDLQSQYL
     NIISRSQATP GPKLKCKILE DMIINKMLLA KADIDSVTVS DAQVEDQLNR RIALLIQQAN
     GSQAELEKLY GKTMDQIKED IRDILKEQLT VQKMNGEITA NVKITPKEVK KYFKNIPKDS
     LPYFQDEVEV GHIVRIPEPT KEQKMIIRQK LEKIRERLLK GEEFGPLAQE FSQDYGSAKQ
     GGNLGWQTRG VFVPKFEATA FRLKKGEISK VIESQLGFHV IQLLDRRGNE FNTRHIFMKP
     DYSLVDVSEA SKFLDSLRTM IAHDSISFAK AAKEYSDDKL TAGNAGILTS PVTGTTQIVV
     KDLDSYLYLT LDTMKVGGIT KPQSYRTNDG KTAVRIIYFK SKIPAHNADF TKDYQKIYTA
     ALNEKKAKAI NQWFNRVKGE MFIQIDKAYK DCNVLNN
//