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Database: UniProt
Entry: A5PC18_9SPHN
LinkDB: A5PC18_9SPHN
Original site: A5PC18_9SPHN 
ID   A5PC18_9SPHN            Unreviewed;       448 AA.
AC   A5PC18;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 66.
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=ED21_30324 {ECO:0000313|EMBL:EDL48588.1};
OS   Erythrobacter sp. SD-21.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=161528 {ECO:0000313|EMBL:EDL48588.1, ECO:0000313|Proteomes:UP000005498};
RN   [1] {ECO:0000313|EMBL:EDL48588.1, ECO:0000313|Proteomes:UP000005498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD-21 {ECO:0000313|EMBL:EDL48588.1,
RC   ECO:0000313|Proteomes:UP000005498};
RA   Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:EDL48588.1}.
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DR   EMBL; ABCG01000005; EDL48588.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5PC18; -.
DR   STRING; 161528.ED21_30324; -.
DR   eggNOG; COG0760; Bacteria.
DR   Proteomes; UP000005498; Unassembled WGS sequence.
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; 2.
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:EDL48588.1}; Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005498};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..448
FT                   /note="Parvulin-like PPIase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007909578"
FT   DOMAIN          198..296
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   448 AA;  48927 MW;  79FDE3D5935C9759 CRC64;
     MNATIVSKLL GLSAAMGLAV AAPATAQSQG PAPQADPLGL PAQPTMLATA NPNVRKATAV
     VNGYVITGTD LDQRLALLVN ANQTEIPAEE LQRVRAQVLR NLIDETLQIQ AAEAEEIVIS
     DAEVEQTFAR VAAQNNQRPE DMENYLASIG SSSASLKRQI RGELAWQRLL RQKVSFFVNV
     SAEEVNELME RLEAAKGTDE YWLWEIFMSA TPENDAAVQA NAQKIMEQLR QGGSFVAYAR
     QFSEASTAAV GGDLDWIHLA QLGDPQLETV VAQMEAGQLV GPIKIPGGYW IVYLRDKRQV
     LMADPRDAML SLKQIQIDFD PAAAPEVNKQ KLDAFTQGVS TMRGCGSADE IASSLGASVV
     TNDQIRARAL PEQLQNIMLS LQIGETTPPF GSLEEGVRVL MLCGRDDPES SEGPNFDELM
     AQIEDERINK AAQRYLRDLR NDAYIEYN
//
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