ID A0A3D8PCV2_9RHOB Unreviewed; 279 AA.
AC A0A3D8PCV2;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Parvulin-like PPIase {ECO:0000256|ARBA:ARBA00018370};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase plp {ECO:0000256|ARBA:ARBA00030642};
DE AltName: Full=Rotamase plp {ECO:0000256|ARBA:ARBA00031484};
GN ORFNames=DIE28_10380 {ECO:0000313|EMBL:RDW13045.1};
OS Paracoccus thiocyanatus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=34006 {ECO:0000313|EMBL:RDW13045.1, ECO:0000313|Proteomes:UP000256679};
RN [1] {ECO:0000313|EMBL:RDW13045.1, ECO:0000313|Proteomes:UP000256679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SST {ECO:0000313|EMBL:RDW13045.1,
RC ECO:0000313|Proteomes:UP000256679};
RA Ghosh W., Rameez M.J., Roy C.;
RT "Whole genome sequencing of Paracoccus thiocyanatus SST.";
RL Submitted (MAY-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:RDW13045.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QFCQ01000053; RDW13045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8PCV2; -.
DR Proteomes; UP000256679; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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 InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
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; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:RDW13045.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000256679};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..279
FT /note="Parvulin-like PPIase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017813741"
FT DOMAIN 133..222
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 279 AA; 30012 MW; 18A01FA95D039A33 CRC64;
MLKPLFAASA LLSGAVLGLP VLAQDADTVV ATVNDESITL GQMIAMRQGL DAHSTQGLPD
TALWDLMLDQ MIRQTAVAQA AQPLSQRDSV ALELEKRAYL AGSVLEKIAE AEPSEAELKA
AYDQAFAGQA EPAIEYSAAH ILVKTKEEAD AIAKQLADGA DFGALAEEKS TDNSGPNKGD
LGWFQPEQMV APFAEAVKAL EKGQVSQPVE TQFGWHVIKL NDTREVTPPA FDEIKEQLAV
QVRRDKVQAE IEKRVADAKI EKTEGLAPDL LNKTDLLGK
//