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Database: UniProt
Entry: A0A0F0KS79_9MICO
LinkDB: A0A0F0KS79_9MICO
Original site: A0A0F0KS79_9MICO 
ID   A0A0F0KS79_9MICO        Unreviewed;       684 AA.
AC   A0A0F0KS79;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE            EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN   Name=f1pep1 {ECO:0000313|EMBL:KJL23324.1};
GN   ORFNames=RL72_02112 {ECO:0000313|EMBL:KJL23324.1};
OS   Microbacterium azadirachtae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL23324.1, ECO:0000313|Proteomes:UP000033448};
RN   [1] {ECO:0000313|EMBL:KJL23324.1, ECO:0000313|Proteomes:UP000033448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL23324.1,
RC   ECO:0000313|Proteomes:UP000033448};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) 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   -!- 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:KJL23324.1}.
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DR   EMBL; JYIT01000077; KJL23324.1; -; Genomic_DNA.
DR   RefSeq; WP_045250783.1; NZ_JYIT01000077.1.
DR   AlphaFoldDB; A0A0F0KS79; -.
DR   PATRIC; fig|582680.7.peg.2159; -.
DR   OrthoDB; 9801421at2; -.
DR   Proteomes; UP000033448; 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   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   Hydrolase {ECO:0000313|EMBL:KJL23324.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033448}.
FT   DOMAIN          7..363
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          469..659
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   684 AA;  73086 MW;  55A5C3DD006167A7 CRC64;
     MSAAPHTRTE DVVEIVAGIA VPDPYRWLEG DASVPGEVAD WQRAQAAYAE ETLWSGHDRD
     AIRALVEHSH EGAWPELPRS GGGLWFRAQG GRLLVADEPY GAGRILLDLR RFDEPGGTAV
     LSWFAPSPDG AVLAVGVCTD GSEHNRVELV DVATGSLRDD APPEPLHSSW GGGISWFPDS
     TGFAFLGLRS PAQDFRQVVY RRELGTRGPS AIEDVPIPDG SREYTRIQFS PDGRWAVAVH
     RVGTPFPVAV RDLSHPGTGW RPFLPPRPET VVGHIVGDRY VTVTDLDAPR RRLVAIPLDA
     EDPADPSGWT ELVPEGEAVL RSVLPVGDAL YLSEFHRTAA RVRILDHDGA ERGVVPLPGQ
     GALAAPFFPL TGLAAESRDG SFVFAFSTLT TSWGVYRHRP GGALEVLQEP RIAIDATAEL
     REATAADGTA IPYHVVRPRG AAAPAPVLIS AYGAAGIPTL PQYQPDLAAV LSAGGTVVQA
     YLRGGGEFGS AWFRAADRER RGTRDGDLLA VAEDVLATGI AAPGRLALSG GSDGGLMCGN
     AITARPDLWC AVLPRAPLLD LVGGFRNPYL EFVIRKAWGD PEDPVDVARM IALSPYERVR
     PAEYPLLYVE AGANDPRCPP WQARKFVARM QAAQRGSAPI LLHVYENAGH GSGTGHDVIV
     AQDAAWLACL LGALGLPDPV APQR
//
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