ID A0A2W2F2P2_9ACTN Unreviewed; 689 AA.
AC A0A2W2F2P2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN ORFNames=C1I98_31760 {ECO:0000313|EMBL:PZG29621.1};
OS Spongiactinospora gelatinilytica.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Spongiactinospora.
OX NCBI_TaxID=2666298 {ECO:0000313|EMBL:PZG29621.1, ECO:0000313|Proteomes:UP000248544};
RN [1] {ECO:0000313|EMBL:PZG29621.1, ECO:0000313|Proteomes:UP000248544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7K107 {ECO:0000313|EMBL:PZG29621.1,
RC ECO:0000313|Proteomes:UP000248544};
RA Sahin N., Saygin H., Ay H.;
RT "Draft genome sequence of Sphaerisporangium sp. 7K107.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC EC=3.4.21.26; Evidence={ECO:0000256|ARBA:ARBA00001070};
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228}.
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:PZG29621.1}.
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DR EMBL; POUA01000369; PZG29621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2F2P2; -.
DR Proteomes; UP000248544; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; IPR002471; Pept_S9_AS.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR PANTHER; PTHR42881:SF2; 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; PS00708; PRO_ENDOPEP_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 7..416
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 474..685
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 75396 MW; 3CD9C10BC212EC4B CRC64;
MTPMPYPPAR RDDQAEELHG IRVPDPYRWL EDPDDPATKE WLDAQQSLFT ATLDTRPAFR
DRIAELLRSG SVGVPVWRGK RSFFMRRTPD QEHSVLYTVD PDGTERVLID PMALDPSGLT
TLDSWQPDKE GRLLAYQISV GGDEESNVYV LDIGSGDRID GPIDRCRYSP IAWLPGGEAF
YYVRRLPASA VPAGEDQYHR RVFLHQVGAP SDEDVEIFGH GMEKTNYYGV GVSRDGRWLT
ISASRGTAPR NDLWMADLAA SRPESPALVT VQEGVDAQTS LHFGRDGRLY VFTDRDAPRG
RVCVTDPQRP GHEHWRDLIP EDPEAVLSDY AILDELGSPV MLVGWTRHAI SEITVHDLAT
GAKTGDVPTP GLGTIGGIIE RPEGGHEAWF SYTDNTTPPT IQRYDARTGQ TTLWASSPGA
VEVPAVKTEQ VVYTSADGTE VHMLVISRPD TTGPRPTILY GYGGFGISMT PGYSASILTW
VEAGGVYAIA QLRGGGEQGE EWHRAGMLAG KPRVYEDLHA AAEHLIATGV TTSATLGISG
GSNGGLLVGA ALTQRPDLYA AVVCSAPLLD MIRYERFGLG ATWNVEYGSA DVVEEFAWLW
SYSPYHHVRE GVSYPATLFS VFASDTRVHP MHAWKMCAAL QHAQADPARP ILLRNETEVG
HGARAVSKSV DLAADQLSFL AQHTGLREG
//
