ID A9BSE4_DELAS Unreviewed; 300 AA.
AC A9BSE4;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=PpiC-type peptidyl-prolyl cis-trans isomerase {ECO:0000313|EMBL:ABX33758.1};
GN OrderedLocusNames=Daci_1113 {ECO:0000313|EMBL:ABX33758.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX33758.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX33758.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) 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; CP000884; ABX33758.1; -; Genomic_DNA.
DR AlphaFoldDB; A9BSE4; -.
DR STRING; 398578.Daci_1113; -.
DR KEGG; dac:Daci_1113; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_9_1_4; -.
DR Proteomes; UP000000784; Chromosome.
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; PTHR47245:SF1; FOLDASE PROTEIN PRSA; 1.
DR PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 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 Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:ABX33758.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000784};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 141..244
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 32073 MW; B369DCE637F59DF8 CRC64;
MEHGCNGSGG GHCGCASSTP SSTSSAPMGD LPAIPEVPAF QPVGEAGAEV ARINNTPLHA
PGQRPPEREL RQRACTELLR QAAQREGLLG ADDAAGDDGV ISERASQAIE QLLEQSLHLP
EPGEDACRRH FDANPARFAQ GERVRLRHVL FAVTPGVDVR ALTQRAEALL IELRCADDAG
LRFAEAARQW SNCPSGQHGG ELGWLGRSDC APEFARDVFA SQEIGVLPRL VHSRFGLHVV
EVCAREAGVL PDWQQARPAV AQALHQQTWV SALHQYLQLL AGQSEVVGVR IAAADSPLVQ
//
