ID A0A0Q5CLC7_9BURK Unreviewed; 719 AA.
AC A0A0Q5CLC7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=ASF61_13335 {ECO:0000313|EMBL:KQQ33058.1};
OS Duganella sp. Leaf126.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ33058.1, ECO:0000313|Proteomes:UP000051032};
RN [1] {ECO:0000313|EMBL:KQQ33058.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ33058.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ33058.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ33058.1};
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 -!- 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:KQQ33058.1}.
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DR EMBL; LMNW01000032; KQQ33058.1; -; Genomic_DNA.
DR RefSeq; WP_056158779.1; NZ_LMNW01000032.1.
DR AlphaFoldDB; A0A0Q5CLC7; -.
DR STRING; 1736266.ASF61_13335; -.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000051032; 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 InterPro; IPR019500; Pep_S46.
DR InterPro; IPR009003; Peptidase_S1_PA.
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}; Hydrolase {ECO:0000256|RuleBase:RU366067};
KW Protease {ECO:0000256|RuleBase:RU366067};
KW Serine protease {ECO:0000256|RuleBase:RU366067};
KW Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 20..719
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023156596"
SQ SEQUENCE 719 AA; 78364 MW; 3C343AA62018C637 CRC64;
MHKTLIALAI LSTTAAAHAD EGMWMPQQLP QVAKQLKAAG LALDPASLTK LTEFPMGAIV
SLGGCSASFV SPQGLVATNH HCVYGSVAHN STPERDLLAN GFLAKTLGEE LPAAPGSRIF
VTKAVTDVSK QIITPAVAKL EGKARLDAIE NNTKTLQAEC EKDAGHRCTV SSFYGGLAFY
LIKQLEIRDV RLVHAPPAGV GKFGGDTDNW MWPRHTGDYG FYRAYVSKDG KAADYSKDNV
PYVPQHYLKL AKQGVKEGDF VMVLGYPGRT NRHRLPSEVA FTFDWSYPAF VKSSAESLAI
IAETTKDNKD TALKYASQVA GINNYYKNRQ GMLDSYAGSD MLARKTAEHE ALKQWINADA
ARKQEYGADI AAVEQLIAER DAETKRDYFL STSKPRLLNT ARMLYRLSNE NTKPDAERKS
GYQVRDVPRI KSSVAALVRN YDEKVDKALV MNSLSKYAAQ PAAERNAAFD SVVGIKDGMS
RADLQAALDK LYAGSKLGDV AVRTAWLDKQ PADFKASDDS FIKAAVALYG PDLKDEEREE
DLAGKLQASY ANYMKAKIAY MNSKGQAVYP DANSTLRVTF GKIAGRKPGS DGTDWKAFTT
VAGVAAKATG TGEFNAPKAQ LDAIKAKQFG NYVDPVLKSV PVAYLATLDI TGGNSGSAAL
NSKGEWIGLA FDGTLDSIIS DWDFNKAMTR SIQVDLRYIL WNMKYVDHAD NLLKEMHAE
//
