ID A0A0T0M548_9FLAO Unreviewed; 709 AA.
AC A0A0T0M548;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=ASG21_02700 {ECO:0000313|EMBL:KQS91406.1};
OS Chryseobacterium sp. Leaf394.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1736361 {ECO:0000313|EMBL:KQS91406.1, ECO:0000313|Proteomes:UP000051822};
RN [1] {ECO:0000313|EMBL:KQS91406.1, ECO:0000313|Proteomes:UP000051822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf394 {ECO:0000313|EMBL:KQS91406.1,
RC ECO:0000313|Proteomes:UP000051822};
RX PubMed=26633631; DOI=.1038/nature16192;
RA Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL Nature 528:364-369(2015).
RN [2] {ECO:0000313|Proteomes:UP000051822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf394 {ECO:0000313|Proteomes:UP000051822};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000051822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf394 {ECO:0000313|Proteomes:UP000051822};
RA Vorholt J.;
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:KQS91406.1}.
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DR EMBL; LMQH01000011; KQS91406.1; -; Genomic_DNA.
DR RefSeq; WP_056076849.1; NZ_LMQH01000011.1.
DR AlphaFoldDB; A0A0T0M548; -.
DR STRING; 1736361.ASG21_02700; -.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000051822; 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|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU366067}; Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 21..709
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023157824"
SQ SEQUENCE 709 AA; 79943 MW; D82E75C80FDEC80C CRC64;
MIKRNILIAS AFFSFSLGFA QQYGGMWIPT ELNEKEMKDL GMKISAKDIF NTQKPSIKDA
VVQFNGGCTA EIISPKGLLL TNHHCGYSQI QSHSTVQNDL LSNGFWAKNS NEELANPGVT
VDFIIDIKDV TKEILEGNPY LDVATINANI QKVQSTTKTE SGQKVMVRPM YYGNKYYAFV
IDTFKDIRLV GAPPQSIGKF GSDTDNWVWP RHTGDFSMFR IYADKNNRPA EYSKDNVPYV
PKHYLPVSIK DKKENDFTFV YGFPGRTTEY LPSIAVDKIM KDTDPARIAG RDVALKTLDE
KMRADDATRI KYASKYASVA NYWKKWIGEV EGLKKSNAVQ KKAAYEQTLT AKNPDIKTTL
DQLNQLYNEQ APYALNNAYY TETIRNAETL TLANLYSSYI TAVESGKMDE KTTASFKNRL
SSFYKDYSAE LDAKVTAKLL ALYANKTAPQ FLPAGFDRYK NEAQNLQTIE SLSKNSVITG
RSEVNGASLS ADIDKAFSNP DKLIKAIKKD EMYILFNSLK DTYTKSADIQ YTSLQAKIDA
LQKKFMAQQM ETDKDRKFFP DANSTMRVTY GKIKGSSPRD AVSYDFQTHL AGVVEKYVPG
DYEFDVPQKL LDLYNKKDYG VYKDKSGDVP VGFTATNHTT GGNSGSPALD AHGNLVGLNF
DRQWEGTMSD INYDPRFSRN IMVDTKYILF IIDKFADSKW LIDEMKIVK
//
