ID A0A0Q6VMY6_9BURK Unreviewed; 714 AA.
AC A0A0Q6VMY6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=ASD15_17080 {ECO:0000313|EMBL:KQV79749.1};
OS Massilia sp. Root351.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV79749.1, ECO:0000313|Proteomes:UP000051876};
RN [1] {ECO:0000313|EMBL:KQV79749.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV79749.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV79749.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV79749.1,
RC ECO:0000313|Proteomes:UP000051876};
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:KQV79749.1}.
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DR EMBL; LMDJ01000033; KQV79749.1; -; Genomic_DNA.
DR RefSeq; WP_057157867.1; NZ_LMDJ01000033.1.
DR AlphaFoldDB; A0A0Q6VMY6; -.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000051876; 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; DIPEPTIDYL-PEPTIDASE; 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}; Hydrolase {ECO:0000256|RuleBase:RU366067};
KW Protease {ECO:0000256|RuleBase:RU366067};
KW Reference proteome {ECO:0000313|Proteomes:UP000051876};
KW Serine protease {ECO:0000256|RuleBase:RU366067};
KW Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 24..714
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023153293"
SQ SEQUENCE 714 AA; 78416 MW; 037B96C94A09EFCA CRC64;
MFKSLAFSAL PAALLAAFSP AHADEGQWQP HQLPQLKAEL KRIGIAIPAE KLADLSKHPM
SAIVSTDGCS ASFVSPDGLV VTNHHCAYGA IQRNSTPEHN YIANGFLAKT RSAELPGGPN
LQVYVTDKVE NVSARVLQGL DKLGGKARHE EAQKRIKALI AECETDKMYR CSVPSFHRGA
EYYRIRQMQI RDVRLVYAPS DKIGNYGGDI DNYEWPRHTG DYSFLRAYVG KDGRPADPSP
DNVPYKSKDF LVVSAEGLKN GDPILLAGYP GRTSRYKLPV EIRNARDSAY PLQAAEYQSD
LDTIAAATKG DAAGEVRYAS VVKSINNRMK KTLGLMDGFA RKDLAAVKDA QDAEFRTWYA
RQPGVSASML SELDAAIAAD MALADEEFAW GVATNSDLLK SARTLYRLAL EKQKPDAERK
AGYQQRDVSP IRARLTRLEQ SFTQKVDQAR YADGLARYAR LAAKSHPQGL DAQLPSVAEV
PALYAQSKLG ATAERLALMD KDAAAIAASD DAFLKLAVKL HAVGLSLEER RMEVDGNLER
VVPQYMAAVI AWKKSQGKPV YPDANSTLRV TYGTVSPYSP KDGLTKGPFT TVEGIVEKHT
GKDPFIAPGN LIDAVKARRY GQFKDPVLGT VPVNFLSSAD TTGGNSGSAV MNKRGELIGL
NFDSTYESIT KDWYFDTAIT RAIHLDIRYM LWVMKEVDHA DNLLQEMTIK YPKK
//