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Database: UniProt
Entry: A0A2S8XX14_9PSED
LinkDB: A0A2S8XX14_9PSED
Original site: A0A2S8XX14_9PSED 
ID   A0A2S8XX14_9PSED        Unreviewed;        91 AA.
AC   A0A2S8XX14;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase C {ECO:0000256|ARBA:ARBA00040926};
DE   AltName: Full=Parvulin {ECO:0000256|ARBA:ARBA00043072};
DE   AltName: Full=Rotamase C {ECO:0000256|ARBA:ARBA00041926};
GN   ORFNames=CQZ98_24525 {ECO:0000313|EMBL:PRA45762.1};
OS   Pseudomonas sp. MYb115.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1848717 {ECO:0000313|EMBL:PRA45762.1, ECO:0000313|Proteomes:UP000239970};
RN   [1] {ECO:0000313|EMBL:PRA45762.1, ECO:0000313|Proteomes:UP000239970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MYb115 {ECO:0000313|EMBL:PRA45762.1,
RC   ECO:0000313|Proteomes:UP000239970};
RA   Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA   Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA   Kaleta C., Schulenburg H.;
RT   "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT   from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:PRA45762.1}.
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DR   EMBL; PCQM01000030; PRA45762.1; -; Genomic_DNA.
DR   RefSeq; WP_027620338.1; NZ_PCQM01000030.1.
DR   AlphaFoldDB; A0A2S8XX14; -.
DR   Proteomes; UP000239970; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   PANTHER; PTHR43629; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR43629:SF3; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE C; 1.
DR   Pfam; PF00639; Rotamase; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000313|EMBL:PRA45762.1};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW   ProRule:PRU00278}.
FT   DOMAIN          1..89
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   91 AA;  10091 MW;  458CF1660868FC0D CRC64;
     MKAQARHILV KTSDEAEQLK QRIAKGEAFD VLAKKFSICP SGKRGGDLGE VRPGQMVGAI
     DAVIFKKPLR VVHGPIKSKF GYHLVQVFFR D
//
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