ID A0A0D6B7K4_RHOSU Unreviewed; 281 AA.
AC A0A0D6B7K4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=NHU_04000 {ECO:0000313|EMBL:BAQ71123.1};
OS Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=35806 {ECO:0000313|EMBL:BAQ71123.1, ECO:0000313|Proteomes:UP000064912};
RN [1] {ECO:0000313|EMBL:BAQ71123.1, ECO:0000313|Proteomes:UP000064912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2351 {ECO:0000313|EMBL:BAQ71123.1,
RC ECO:0000313|Proteomes:UP000064912};
RA Nagao N.;
RT "Genome sequene of Rhodovulum sulfidophilum DSM 2351.";
RL Submitted (FEB-2015) 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; AP014800; BAQ71123.1; -; Genomic_DNA.
DR RefSeq; WP_060836125.1; NZ_AP014800.1.
DR AlphaFoldDB; A0A0D6B7K4; -.
DR KEGG; rsu:NHU_04000; -.
DR PATRIC; fig|35806.4.peg.4101; -.
DR eggNOG; COG0760; Bacteria.
DR Proteomes; UP000064912; Chromosome.
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; IPR023058; PPIase_PpiC_CS.
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; 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:BAQ71123.1};
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..281
FT /note="Parvulin-like PPIase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007764663"
FT DOMAIN 134..223
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 281 AA; 30391 MW; 7C7FD15144176A89 CRC64;
MSFALRPLAV LALGATLALP ALADEIGPDT VVARVGDQEI TIGHMIVLRA QLPAEYQQLP
DDVLYQAVLD QLIRQTAVGE AIGKELSTGA RLALENERRS FVAGEALSRL AEAAVTDEAV
EAAYNATYGE ADPTNEYHAA HILVETEDEA QAIEAQLGDG ADFAQLAKEK STGPSGPNGG
DLGWFSEGMM VKPFEEAVTV LEPGEVSAPV QTQFGWHVIK LYETRLKDAP RLADVRGELV
QQIQRDAMEE ALEKYTEEAD VSRPEIEVDP AILKDQSVLD R
//
