ID   U1MSE2_9MICO            Unreviewed;       684 AA.
AC   U1MSE2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE            EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN   ORFNames=L332_03820 {ECO:0000313|EMBL:ERG63580.1};
OS   Agrococcus pavilionensis RW1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agrococcus.
OX   NCBI_TaxID=1330458 {ECO:0000313|EMBL:ERG63580.1, ECO:0000313|Proteomes:UP000016462};
RN   [1] {ECO:0000313|EMBL:ERG63580.1, ECO:0000313|Proteomes:UP000016462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RW1 {ECO:0000313|EMBL:ERG63580.1,
RC   ECO:0000313|Proteomes:UP000016462};
RX   PubMed=23814108;
RA   White R.A.III., Grassa C.J., Suttle C.A.;
RT   "First draft genome sequence from a member of the genus agrococcus,
RT   isolated from modern microbialites.";
RL   Genome Announc. 1:e00391-13(2013).
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   -!- 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:ERG63580.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ASHR01000030; ERG63580.1; -; Genomic_DNA.
DR   RefSeq; WP_021011038.1; NZ_ASHR01000030.1.
DR   AlphaFoldDB; U1MSE2; -.
DR   OrthoDB; 9801421at2; -.
DR   Proteomes; UP000016462; 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; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016462}.
FT   DOMAIN          4..385
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          464..680
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   684 AA;  73508 MW;  90F7DE4D1519940D CRC64;
     MRYPEVRRDG TVETVHGEAI PDPYRWLEDG DAAETRAFIE AQNAFAEPIL AALPAREAFR
     ERVAALLTAP TRGCPWERGG RVFAWHGGEQ NQPVLVVADA VDELERGRVL LDPNALSADG
     TVAVNVASVS PDGALLAYGV SDGGSDWRTI RVRDVATGDD LADEIPWTKW NPPVWLPGGR
     AFSYWAYDAP TGDALTDEMG AGRLMRHEIG ADPSTDAVLF ARPDEPRLFA RHWPRDDEWF
     VLSTDTGSSS GNDLAVRRHG DEAAALRQLV EGHEHEWSAI GIHGGRLFAV TDESAPRYRL
     AAFDLETGEQ STIVPEHEED VLLDASLTER GLVLEYSHDA SHRMQLASLE GELGDAVPLG
     DGVSITGSEA SSGTGTVFAS TSSFVDRGTR HVIVVDGARL VEHRALLAPG PAAPRAATHR
     IRTASSDGQQ VPAFLVRPAG DAGDAPRPTL IWGYGGFNIP MNPAFRAVLA AWVEAGGVLV
     VPNLRGGGEF GSEWHKGGTK ERKQQVFDDL FAIAEHLIAT GVTTREQLAL HGRSNGGLLA
     GAALTQRPEL WAAVLPGVGV LDMLRYHRFT IGWAWASDYG DPDDAEAHAY LRAYSPLHNV
     RDGVAYPPTL ITTGDHDDRV VPAHSFKFAA ELQRAQAATG ADAPVLLSVD TRAGHGMGKP
     KDAAALEFAD QLAFAAHHTG LDVR
//