ID A0A0K8P5U6_IDESA Unreviewed; 735 AA.
AC A0A0K8P5U6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Prolyl endopeptidase {ECO:0000313|EMBL:GAP37961.1};
DE EC=3.4.21.26 {ECO:0000313|EMBL:GAP37961.1};
GN ORFNames=ISF6_4155 {ECO:0000313|EMBL:GAP37961.1};
OS Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Piscinibacter.
OX NCBI_TaxID=1547922 {ECO:0000313|EMBL:GAP37961.1, ECO:0000313|Proteomes:UP000037660};
RN [1] {ECO:0000313|Proteomes:UP000037660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC {ECO:0000313|Proteomes:UP000037660};
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "Discovery of a poly(ethylene terephthalate assimilation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAP37961.1, ECO:0000313|Proteomes:UP000037660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC {ECO:0000313|Proteomes:UP000037660};
RX PubMed=26965627; DOI=10.1126/science.aad6359;
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "A bacterium that degrades and assimilates poly(ethylene terephthalate).";
RL Science 351:1196-1199(2016).
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:GAP37961.1}.
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DR EMBL; BBYR01000064; GAP37961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K8P5U6; -.
DR STRING; 1547922.ISF6_4155; -.
DR Proteomes; UP000037660; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR PANTHER; PTHR42881:SF13; PROLYL ENDOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:GAP37961.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037660};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..735
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005513742"
FT DOMAIN 48..448
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 526..729
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 29..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 735 AA; 80825 MW; C6ACCEE136B4611C CRC64;
MSDSLPSPRR RALAAAGLAS LLGPLPRTAM SQAASAPATP PPAAPVPDDP FRWLEDVQGD
KSLAWVRERN AASQAVLGTR PEFEPIRREL LEVLNAKDRI PAVTRRGAWL YNLWQDEQHK
RGLWRRTTLA EYRKPQPAWE TVLDLDALGA AEKENWVWGG AVALAPEYRR CLVALSRGGA
DATVVREFDT VTKRFVDGGF TLPEAKSEVD WIDADTVYVA TDFGAGSLTD SGYPRVIKRW
KRGTPLSDAQ TVFEGQASDV SVSVGIDDTP GHERTQFYRA TDFYNRKTFL LPHGAEPKAM
QPLDVPDDAV VGFMRDTLLL ELRSDWTVGG TRHPAGSLLA ADAAAYLKGE RRFQVLFTPT
PTRSLSGRIQ TRDHLVLNLI DNVASTLAMW HKTPQGFVSV PIEAPTPGSL GLASLHDPRV
PKDPLANHYL LTYTDFLTPD TLYLGDTTAA PQAPRERLKQ RQPLFDATGM RAEQRFARSK
DGTRVPYFVV WPKGAQADGR TPTLLYGYGG FKISLKPWYS GGFGRAWLSR GGALVIANIR
GGGEFGPAWH QAAVKANKQR SYDDFIAVAE DLVAAKVTSP RHLGIMGGSN GGLLVGATMV
QRPDLFNAVV CQVPLLDMRR YNVLLAGASW MAEYGNPDLP AEWAWISGYS PYQNVKPGVK
YPKVLFTTST RDDRVHPGHA RKMAARMLAQ GHEVLYYENI EGGHGGAADN EQRAYLQSLE
YAYLWQQLGP AGRGG
//