ID A0A240U1C1_9BURK Unreviewed; 261 AA.
AC A0A240U1C1; A0A240UE86;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Peptidylprolyl isomerase {ECO:0000313|EMBL:ART51655.1};
GN ORFNames=CBP34_08285 {ECO:0000313|EMBL:ART51655.1}, CBP36_11625
GN {ECO:0000313|EMBL:ART59405.1};
OS Acidovorax carolinensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=553814 {ECO:0000313|EMBL:ART51655.1, ECO:0000313|Proteomes:UP000194432};
RN [1] {ECO:0000313|Proteomes:UP000194432, ECO:0000313|Proteomes:UP000194440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA3 {ECO:0000313|EMBL:ART51655.1}, and P4
RC {ECO:0000313|EMBL:ART59405.1};
RA Singleton D.R., Lee J., Dickey A.N., Stroud A., Scholl E.H., Wright F.A.,
RA Aitken M.D.;
RT "Polyphasic characterization of four soil-derived phenanthrene-degrading
RT Acidovorax strains and proposal of Acidovorax phenanthrenivorans sp. nov.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC {ECO:0000256|ARBA:ARBA00007656}.
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DR EMBL; CP021361; ART51655.1; -; Genomic_DNA.
DR EMBL; CP021366; ART59405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A240U1C1; -.
DR KEGG; acin:CBP34_08285; -.
DR KEGG; acip:CBP36_11625; -.
DR KEGG; acis:CBP35_07300; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000194432; Chromosome.
DR Proteomes; UP000194440; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.1040; -; 1.
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; PF13616; Rotamase_3; 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:ART51655.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000194432};
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..261
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033294419"
FT DOMAIN 131..222
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 261 AA; 28867 MW; D181763E3621AB02 CRC64;
MKKQLLSGLV AAAVLGSMAL PVSAQNIAIV NGKAVPKERA EVLRQQVERS GRPVTPEMEG
QIKEEVIARE IFLQEAQKRG LEASPEYKAQ MELARQTILI RELFADFQKN NPVTDAEIQA
EYDKFAAANS GKEYKASHIL VDKEADAKAI IASIKKGAKF EDIAKKQSKD PGSGAKGGDL
DWANPASYVT EFTEALIKLS KGKMTDTPVK SQFGWHVIRL DDTRQAQLPK LEEVKPQVAQ
QLQQQKLAKF QEDLRAKAKV E
//
