ID   A0A369AM83_9BURK        Unreviewed;       278 AA.
AC   A0A369AM83;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Peptidyl-prolyl cis-trans isomerase C {ECO:0000313|EMBL:RCX10175.1};
GN   ORFNames=DFR45_103160 {ECO:0000313|EMBL:RCX10175.1};
OS   Extensimonas vulgaris.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Extensimonas.
OX   NCBI_TaxID=1031594 {ECO:0000313|EMBL:RCX10175.1, ECO:0000313|Proteomes:UP000252174};
RN   [1] {ECO:0000313|EMBL:RCX10175.1, ECO:0000313|Proteomes:UP000252174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100911 {ECO:0000313|EMBL:RCX10175.1,
RC   ECO:0000313|Proteomes:UP000252174};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC       {ECO:0000256|ARBA:ARBA00007656}.
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:RCX10175.1}.
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DR   EMBL; QPJU01000003; RCX10175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369AM83; -.
DR   OrthoDB; 9769613at2; -.
DR   Proteomes; UP000252174; 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   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR023058; PPIase_PpiC_CS.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   PANTHER; PTHR47245:SF1; FOLDASE PROTEIN PRSA; 1.
DR   PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR   Pfam; PF00639; Rotamase; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000313|EMBL:RCX10175.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252174};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          115..222
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   278 AA;  30048 MW;  0F7EB096499FBB37 CRC64;
     MKPHTSTVTG CGHAACACTG APSAPARING VALHRTDEHH GADALRERAY AELLRQEAVR
     AGLLPALDTA LAPELDAAER AVIESMVERA VASPQPTPEE VRRYYEANPQ QFMQGQAVHL
     RHILFAVTPG VNVHALTVRA EQALLELVGK DAPAPRFAEL AAELSNCPSG AQGGDLGWVA
     PEDCAPELAN ELFQQKHAQW GLGVHPRLVH TRYGFHIIEV LERRKGKLAS FDHVRDRIAA
     QLALQSRARA LHQYMLLLAG QAEVEGIDLG AAQTPLVQ
//