ID A1B0G6_PARDP Unreviewed; 423 AA.
AC A1B0G6;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 105.
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 OrderedLocusNames=Pden_0899 {ECO:0000313|EMBL:ABL69010.1};
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL69010.1, ECO:0000313|Proteomes:UP000000361};
RN [1] {ECO:0000313|Proteomes:UP000000361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000489; ABL69010.1; -; Genomic_DNA.
DR AlphaFoldDB; A1B0G6; -.
DR STRING; 318586.Pden_0899; -.
DR EnsemblBacteria; ABL69010; ABL69010; Pden_0899.
DR KEGG; pde:Pden_0899; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_11_2_5; -.
DR OrthoDB; 9791746at2; -.
DR Proteomes; UP000000361; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; -; 1.
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; 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; 1.
DR Pfam; PF09312; SurA_N; 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 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:ABL69010.1}; Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..423
FT /note="Parvulin-like PPIase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007908983"
FT DOMAIN 165..262
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 368..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 45949 MW; 6CAF567279C4C1E6 CRC64;
MRRILLGAAM AAMLAAGGVA PAFAQGNPFQ PLVYVNDSVV TRYELDQRMR FLQILRAPDG
DRASAEQALI DDRLRLFAAR QMGIAASDAQ IDAGLAEFAG RANMDVEEFT RALAQAGVEQ
QTFRDFIAAG VVWRELVRQR LVPQVQVSDA ELDQEMQRVI ETPRITHVAL SELIIPAPPG
QEAQAMRLAE SLVQSVRSEA DFAAAARQHS ATPSAENGGR LPWAPLENLP PSLRPIILSM
QNGQISQPLT VEGAVVLFYL RDSRGTLRPG AKEQVLDYVR FRLASTAEAN RIAALSDTCA
DLFVHARNLP PEQIQRQTLS QGQIPTAEAI RLAVLDDNES TIVSQGGSAE ILMLCKRQSA
LLAGNAQEAP VPVTAEGEEG AAPDPDALPD REQMRGQIFS RKVGQAADNY LAELRANAII
RRP
//
