ID   A4T2K5_MYCGI            Unreviewed;       668 AA.
AC   A4T2K5;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Peptidase S9, prolyl oligopeptidase active site domain protein {ECO:0000313|EMBL:ABP45104.1};
GN   OrderedLocusNames=Mflv_2627 {ECO:0000313|EMBL:ABP45104.1};
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP45104.1};
RN   [1] {ECO:0000313|EMBL:ABP45104.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP45104.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABP45104.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP45104.1};
RX   PubMed=23469141;
RA   Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT   "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT   Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT   during Pyrene Degradation.";
RL   PLoS ONE 8:E58066-E58066(2013).
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DR   EMBL; CP000656; ABP45104.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4T2K5; -.
DR   STRING; 350054.Mflv_2627; -.
DR   ESTHER; mycgi-a4t2k5; Prolyl_oligopeptidase_S9.
DR   KEGG; mgi:Mflv_2627; -.
DR   eggNOG; COG0823; Bacteria.
DR   eggNOG; COG1506; Bacteria.
DR   HOGENOM; CLU_008615_1_0_11; -.
DR   OrthoDB; 262125at2; -.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR   PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          443..654
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   668 AA;  72156 MW;  193712A50D88A8C9 CRC64;
     MTAAPDPNPV SPTPFHDLDE FLSLPRVSGL AVSRDGARVV TTVATLNDTR TEFVSALWEL
     DPVGREPARR ITRGVTGESA PEFTADGDLL FLAARPTADD DKPPKSLWCL PVAGGEAYEV
     CQMPGGVDGV ASAGGATVVV SSMLPSAVDI DADERLRTAR KDNKVSALLH TGYPVRAWDH
     DIGPARTHLF DADTKRDVTP DPGDALRDSH FDVSPDGGFL VASWNVPAPG AALRSTLVRI
     DVNTGDRAVI VDDPESDAGF PAIAPDGTSV AYLRETLSTP HHAPRITLAL LHFGEEPREL
     TAHWDRWPTS VTWSADGSTL LVTADDDGRG PIFAVDPQTG AVRTLVSDDY TYTDVRAAPG
     GVIFALRSSY AAPQHPVRID PDGTITVLDC VPLPSLPGTL TEIEATAADG QRVRSWLVLP
     EGDHPAPLLL WIHGGPLASW NAWHWRWNPW LMAAGGYAVL LPDPALSTGY GQEFIERGWG
     AWGFAPYTDL MAATDAACAH PRIDETRTAV MGGSFGGYMA NWIAGHTDRF AAIVTHAGLW
     ALDQFGATTD GSYWWSREMT PKMASANSPH LFVSDIRTPM LVIHGDKDYR VPIGEALRLW
     YDLLSRSGLP AADSGPEAGT TQHRFLYFPS ENHWILSPQH AKLWYQVVLG FLNLHVLGQD
     ADVPELLG
//