ID A0A0U4F584_9BACI Unreviewed; 667 AA.
AC A0A0U4F584;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:ALX48758.1};
GN ORFNames=AOX59_09085 {ECO:0000313|EMBL:ALX48758.1};
OS Lentibacillus amyloliquefaciens.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=1472767 {ECO:0000313|EMBL:ALX48758.1, ECO:0000313|Proteomes:UP000050331};
RN [1] {ECO:0000313|EMBL:ALX48758.1, ECO:0000313|Proteomes:UP000050331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAM0015 {ECO:0000313|EMBL:ALX48758.1,
RC ECO:0000313|Proteomes:UP000050331};
RA Wang J.-L., He M.-X.;
RT "Complete genome sequence of strain Lentibacillus amyloliquefaciens
RT LAM0015T isolated from saline sediment.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP013862; ALX48758.1; -; Genomic_DNA.
DR RefSeq; WP_068444892.1; NZ_CP013862.1.
DR AlphaFoldDB; A0A0U4F584; -.
DR STRING; 1472767.AOX59_09085; -.
DR KEGG; lao:AOX59_09085; -.
DR OrthoDB; 108903at2; -.
DR Proteomes; UP000050331; 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 InterPro; IPR002469; Peptidase_S9B_N.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF07676; PD40; 2.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000050331}.
FT DOMAIN 208..345
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 455..665
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 131..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 75571 MW; CF26A73DF668E791 CRC64;
MTNQSKRALT AEDLQQINVY SDPQFAPDGS AYAFVSTKAN DDDDYTSQLF VQSLKNKDAR
QWTFDKAKNS HPRFSPDGKK LIFQSNRSGT PQLWLLQTDG GEARQLTSFK HGALNPAFSK
DGSSIIFSAP LEKNDDATDQ HEQSSDERQK EQNEKSKQPL VINQLNYKSD ASGLLDHKHM
QIVLYNMGND TFEQLTSAET DHNFEDISPD GNYILFSANL HEDRDYELTS DLHLLNVATK
DITTLTNGKG QYGNARFSPD GAKIACFGHE FAFQGATLND LYVFDAASGK SSCLSKLWDF
QLGDVMIGDT RLGQSENGPV WSKDGQHLYF LGTDSGATGL YQADLNGKLN ELYNDNNHVF
GFSLHDGVFI LGISTPSDPG NFYQMTESQL LQLTDANREF LKNVQLSEPE ALTFTADDNW
KIHGWLLRPY GFDENKKYPL ILEVHGGPHA MYGRTFFYEL QLLAAKGYVV LYTNPRGSHG
YGQTFVDACR EDYGGQDYSD LMSAVDYVLD THDFIYRNRL GVTGGSYGGF MTNWIIGHTD
RFKAAVTQRC ISNWLSFYGV SDIGYFFTKW ELGKNLLEDP AKLWEFSPLK YAENIDTPLL
IVHGEKDLRC PIEQSEQLFV TLKHMKKDVE FVRFPDANHE LSRSGKPEMR ISRLNHITRW
FDEHLRI
//
