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Database: UniProt
Entry: A0A0S8ZJ40_9PSED
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ID   A0A0S8ZJ40_9PSED        Unreviewed;        93 AA.
AC   A0A0S8ZJ40;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=ASE98_19910 {ECO:0000313|EMBL:KQN53353.1};
OS   Pseudomonas sp. Leaf48.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1736221 {ECO:0000313|EMBL:KQN53353.1, ECO:0000313|Proteomes:UP000051774};
RN   [1] {ECO:0000313|EMBL:KQN53353.1, ECO:0000313|Proteomes:UP000051774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf48 {ECO:0000313|EMBL:KQN53353.1,
RC   ECO:0000313|Proteomes:UP000051774};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN53353.1, ECO:0000313|Proteomes:UP000051774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf48 {ECO:0000313|EMBL:KQN53353.1,
RC   ECO:0000313|Proteomes:UP000051774};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQN53353.1}.
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DR   EMBL; LMLH01000006; KQN53353.1; -; Genomic_DNA.
DR   RefSeq; WP_060540635.1; NZ_LMLH01000006.1.
DR   AlphaFoldDB; A0A0S8ZJ40; -.
DR   STRING; 1736221.ASE98_19910; -.
DR   OrthoDB; 14196at2; -.
DR   Proteomes; UP000051774; 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   PANTHER; PTHR43629; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR43629:SF2; RHODANESE-LIKE/PPIC DOMAIN-CONTAINING PROTEIN 12, CHLOROPLASTIC; 1.
DR   Pfam; PF13616; Rotamase_3; 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:KQN53353.1};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278}.
FT   DOMAIN          1..90
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   93 AA;  9812 MW;  63CC6789B35E3C99 CRC64;
     MAKASARHIL VASEAKCNEL KAQIEGGADF GEVAKANSTC PSSRQGGDLG SFGPGQMVKE
     FDTVVFSAPL NVVQGPVKTQ FGYHLLEVTS RQD
//
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