ID A0A0Q7PKV1_9GAMM Unreviewed; 719 AA.
AC A0A0Q7PKV1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=ASD14_03230 {ECO:0000313|EMBL:KQY51717.1};
OS Lysobacter sp. Root494.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1736549 {ECO:0000313|EMBL:KQY51717.1, ECO:0000313|Proteomes:UP000051738};
RN [1] {ECO:0000313|EMBL:KQY51717.1, ECO:0000313|Proteomes:UP000051738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root494 {ECO:0000313|EMBL:KQY51717.1,
RC ECO:0000313|Proteomes:UP000051738};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY51717.1, ECO:0000313|Proteomes:UP000051738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root494 {ECO:0000313|EMBL:KQY51717.1,
RC ECO:0000313|Proteomes:UP000051738};
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 -!- FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of
CC oligopeptides. {ECO:0000256|RuleBase:RU366067}.
CC -!- SIMILARITY: Belongs to the peptidase S46 family.
CC {ECO:0000256|ARBA:ARBA00010491, ECO:0000256|RuleBase:RU366067}.
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:KQY51717.1}.
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DR EMBL; LMFH01000005; KQY51717.1; -; Genomic_DNA.
DR RefSeq; WP_056128998.1; NZ_LMFH01000005.1.
DR AlphaFoldDB; A0A0Q7PKV1; -.
DR STRING; 1736549.ASD14_03230; -.
DR Proteomes; UP000051738; Unassembled WGS sequence.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR019500; Pep_S46.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR PANTHER; PTHR38469; -; 1.
DR PANTHER; PTHR38469:SF1; PERIPLASMIC PEPTIDASE SUBFAMILY S1B; 1.
DR Pfam; PF10459; Peptidase_S46; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU366067}; Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|RuleBase:RU366067};
KW Protease {ECO:0000256|RuleBase:RU366067};
KW Reference proteome {ECO:0000313|Proteomes:UP000051738};
KW Serine protease {ECO:0000256|RuleBase:RU366067};
KW Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 23..719
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023156056"
FT COILED 314..348
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 719 AA; 79198 MW; 2464B2737C9F20A8 CRC64;
MPTIRRRLLG LSLSLLGANA HADEGMWMPS QLPDLAREMK AAGFKGDPRD LAELAKPPMS
AVVKVGGASG AFVSDQGLVL TNHHVAFGVI QYNSKPGRDL IRDGYIANTR ADELPSNPDY
RVLVTTGFDR ITDRILGDAK GKQGRAYYDA VDAATKRVVA QCEREAGYRC SVANMYYGTD
FYLVRQLELR DVRLVYAPPN DIGNYGGEVD NFVWPRHAGD FTLLRAYVGK DGKPGDYSPD
NVPYVPSAHL QVSTANLKEG DYAMLAGYPG VTFRHRMASE FAQQIEWQLP SRVALYQRMI
DVVEGAAAKD EAARVSYASQ VRSLKNNLKR AQGELDGLRR SNAAAVRRND EAAMYAWLDR
QSDATTTKAD IAAAQAVLDR AAAMRERDQL LGVIVSQSQL LKSAVTLQRL AHERTKPDAQ
RESGFQQRDE ALIAGQLKQV QRRYAADVEK ALLTELLAQY EALPAAQHVP EFDTVFGTTP
AQLKTKLDAL YAGTQLGAES QRLAAMQADR ATLATSKDSL LQAANALLPA LLRIEEEKKA
SEGELLRLRP AYMRALIGFR KSQGRAVYPD ANSTLRVSYG RVSALDPRDG VHYTPLTTVQ
GILEKHTGEE PFNAPQPLRD AIAKGDFGST AEPTLKTQTV DFLTNLDTTG GNSGSAVMDA
YGKLIGLNFD SNWEAVSASW MFDPRYKRAI HVDMRYMRWL LAKVYPAPHL LKEMNLPAE
//
