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Database: UniProt
Entry: C3FX98_BACTU
LinkDB: C3FX98_BACTU
Original site: C3FX98_BACTU 
ID   C3FX98_BACTU            Unreviewed;       654 AA.
AC   C3FX98;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Acylamino-acid-releasing enzyme {ECO:0000313|EMBL:EEM73691.1};
GN   ORFNames=bthur0009_1610 {ECO:0000313|EMBL:EEM73691.1};
OS   Bacillus thuringiensis serovar andalousiensis BGSC 4AW1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=527032 {ECO:0000313|EMBL:EEM73691.1};
RN   [1] {ECO:0000313|EMBL:EEM73691.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGSC 4AW1 {ECO:0000313|EMBL:EEM73691.1};
RX   PubMed=22645259; DOI=10.1101/gr.134437.111;
RA   Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA   Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA   Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT   "Genomic characterization of the Bacillus cereus sensu lato species:
RT   Backdrop to the evolution of Bacillus anthracis.";
RL   Genome Res. 22:1512-1524(2012).
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:EEM73691.1}.
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DR   EMBL; ACNG01000007; EEM73691.1; -; Genomic_DNA.
DR   RefSeq; WP_000868454.1; NZ_CM000754.1.
DR   AlphaFoldDB; C3FX98; -.
DR   ESTHER; bacce-BC0192; ACPH_Peptidase_S9.
DR   HOGENOM; CLU_008615_2_1_9; -.
DR   Proteomes; UP000001380; Chromosome.
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; 2.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR011659; PD40.
DR   InterPro; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR   PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR   Pfam; PF07676; PD40; 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          446..643
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   654 AA;  74389 MW;  EAB041716383A49C CRC64;
     MKVSEKTYLS IEEIISLPTL SSTNISDDGK NVAFVKKTAN WEDSTYRNHV WIYEKGKGQS
     YPLTTGDIDS IHPFWSPDSK SIAYLSSGGD GDMKNQIFVK SLDDYSEVKI TDEKEGVSNF
     KWNPTGKGFY YITQSKECEE IKKRKELYGD FQHVGKEHQN NCLCYIEIEK VIQNDKEERE
     INGVYQLTDG KDFYIHGFDI SDNGKKVVCM ATPSLNDHMN GDLYILDVEA GELQQMNVDK
     LLDGSVCFSP EGNKICYSAS IREKEYYRNH IQESTLEIYD MNTGEVIQPL TNFDSTVMPL
     QWTAKGILIR WQDKTNYFIG LLAEDGTVET LREKVDGFIM DASITRDGNH ITYNKAITNE
     TFEIYLDDKK ITNENSLFEG KLKSNREIIS WRSSDGLEIE GVLSTPVEFD ANKKYPLLVV
     IHGGPAWASF PIFSNCFNEK YPIEQFVEKG FIVLEPNYRG SSGYGNEFLK ANYRKQGLAD
     YDDVISGVDE LVEKGMVDKD RVGVMGWSNG GYISAFCSTF SSRFKAISVG GGITNWSTHY
     VNTDIPYFIR MYLGNTPWND PDIYKRTSPM TYIKSACTPT LIQHGEKDAR IPITNAYELH
     QGLKDMEVDT ELIIFKGMAY SSDQPGVHVA IMKQNLMWFS HYILGESMED FSTI
//
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