ID A0A091AQM7_9GAMM Unreviewed; 718 AA.
AC A0A091AQM7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, 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=N789_05995 {ECO:0000313|EMBL:KFN41427.1};
OS Arenimonas oryziterrae DSM 21050 = YC6267.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Arenimonas.
OX NCBI_TaxID=1121015 {ECO:0000313|EMBL:KFN41427.1, ECO:0000313|Proteomes:UP000029385};
RN [1] {ECO:0000313|EMBL:KFN41427.1, ECO:0000313|Proteomes:UP000029385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC6267 {ECO:0000313|EMBL:KFN41427.1,
RC ECO:0000313|Proteomes:UP000029385};
RA Chen F., Wang G.;
RT "Genome sequencing of Arenimonas oryziterrae.";
RL Submitted (SEP-2013) 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:KFN41427.1}.
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DR EMBL; AVCI01000045; KFN41427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091AQM7; -.
DR STRING; 1121015.GCA_000420545_00465; -.
DR PATRIC; fig|1121015.4.peg.2861; -.
DR eggNOG; COG3591; Bacteria.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000029385; 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}; Hydrolase {ECO:0000256|RuleBase:RU366067};
KW Protease {ECO:0000256|RuleBase:RU366067};
KW Reference proteome {ECO:0000313|Proteomes:UP000029385};
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..718
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023144650"
SQ SEQUENCE 718 AA; 78042 MW; 7322AB0AE937F69C CRC64;
MRRLVLSSSI ALSLTLSFAA QANEGMWVPQ QLPEIAGPLK QAGLKLDAKQ LADLTGQPMG
AVVAINGCTA SFVSPQGLIA TNHHCAYGSI QLNSTPERNL IRDGFNAAQL GDEVSAGPNA
RVYVMDQITD VTAQVLAEVA PTLDGLARQK AIETAQKALV AACEAEPGYR CTVYSFFGGL
QYRLFRQIEL KDVRLVYAPP ASIGNYGGEV DNWMWPRHTG DFSLIRAYVG KDGKPAAFSA
DNVPYQPKHF LPFTHTPLRP GDFVMVAGFP GSTNRYALAD EFDNTAGWSY PTVGAHLKHV
RDLVHAAGEK NPDIAIKYAS TVKSWENVLK NYDGQLAGFA RVNAAASKRK EENALLAWLA
TRGDAGKPAL EAHDKIVALI AQTRSTRERD LVVGQIVGLG TLGSARSLYR LSIEKAKPNA
ERSPGYQDRD LPRIEGGLKE LQQRYHPDME KQLMTYWLSQ YIQLPASQRI AAVDTWLGGN
DAAAVTRAVD TLYAGSQMGD VGKRLEWFKA DKAAFEASTD PMIRLAVALT PTLMKLEDEG
KARTGENLRY RPVYLAAVQD YKRSKGEGVY PDANSSLRIT YGNVTGYGAK GSATFEPFTT
AEGMAAKATG QDPFNAPQAI LDAVSAKRYG SHADAKLGTL PVNFLSNLDI TGGNSGSPVM
NARGELVGLA FDGNWESVSS NWVFDGTYNR MISVDSRYIT WIMEQVYPAP RLLKEIGM
//
