ID A0A0Q5E723_9BURK Unreviewed; 661 AA.
AC A0A0Q5E723;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Dipeptidyl aminopeptidase {ECO:0000313|EMBL:KQQ47774.1};
GN ORFNames=ASF61_02235 {ECO:0000313|EMBL:KQQ47774.1};
OS Duganella sp. Leaf126.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ47774.1, ECO:0000313|Proteomes:UP000051032};
RN [1] {ECO:0000313|EMBL:KQQ47774.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ47774.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ47774.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ47774.1};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQQ47774.1}.
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DR EMBL; LMNW01000001; KQQ47774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q5E723; -.
DR STRING; 1736266.ASF61_02235; -.
DR OrthoDB; 4269629at2; -.
DR Proteomes; UP000051032; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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; 2.115.10.10; Tachylectin 2; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR42776:SF27; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 6; 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 Aminopeptidase {ECO:0000313|EMBL:KQQ47774.1};
KW Hydrolase {ECO:0000313|EMBL:KQQ47774.1};
KW Protease {ECO:0000313|EMBL:KQQ47774.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..661
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006247705"
FT DOMAIN 443..658
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 661 AA; 72478 MW; 411E929C5012326B CRC64;
MAGGICAAVL ALTAAPAGAA AAAAAPPPIA AFFSNPAFNG AMLSPNGRYL AAFIGAEGRH
DGLAVVDLAD MQAQMVAQFA DTDIGEARWV NNDRLVFSTV DKSLGRRDVR FAPGIFAVNR
NGKQFRQLAM RNNQFVRDGN ATEMLPWHTY MMDQDGPQDS DDIYVMDNGI IAPGILVSVD
LLRLNTKNGT WRGVDHPGTG RDWLLDNKGE PRLMHTLDKN IHAIHYRDPA SGTWRQLTSF
DAYTGGKQAF TPLAFGPDGT LYVVANNGSD HSQLYRYDLQ NNKLGQSLVA LDGFDFRGHL
VISRNTLLGV RVNGDAEGTT WFDPAMKALQ QKIDARLPGM VNLITPPKAP ETAWVLVESY
SDRQPRRFLV FNTETGKLSE VGNLAPAIKP AAMGPRDLVY YKARDGLTIP AWLTLPPGGK
DKNLPMVVLV HGGPFLRGGY WNWNADAQFL ASRGYAVLEP EFRGSTGYGN AHFVAGWKQW
GLKMQNDIAD GTRWAIAQGT ADARRICIAG ASYGGYATLM GLINDPDLYR CGIDWVGVTD
IDLMYNSGWR YSSDLSADWK QYGMPELVAD QVGDAAQIRA TSPLRRAAEI RQPLLLAYGG
ADVRVPLSHG IEFYNAVRKT NADVEWIEYP EEGHGWALPK NRIDFWGRVE KFLDKQIGAA
P
//
