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Database: UniProt
Entry: R5PTL8_9BACT
LinkDB: R5PTL8_9BACT
Original site: R5PTL8_9BACT 
ID   R5PTL8_9BACT            Unreviewed;       707 AA.
AC   R5PTL8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=BN465_01574 {ECO:0000313|EMBL:CCZ12287.1};
OS   Prevotella sp. CAG:1092.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262919 {ECO:0000313|EMBL:CCZ12287.1, ECO:0000313|Proteomes:UP000017987};
RN   [1] {ECO:0000313|EMBL:CCZ12287.1, ECO:0000313|Proteomes:UP000017987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:1092 {ECO:0000313|Proteomes:UP000017987};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCZ12287.1}.
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DR   EMBL; CAZL010000276; CCZ12287.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5PTL8; -.
DR   STRING; 1262919.BN465_01574; -.
DR   Proteomes; UP000017987; 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:UP000017987};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}; Signal {ECO:0000256|RuleBase:RU366067}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT   CHAIN           24..707
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5022995164"
SQ   SEQUENCE   707 AA;  80891 MW;  58A0C21AF6CE6A7D CRC64;
     MKKKATVLIA SMMAFCGLNT AHADEGMWTI YNLPNAVYNI MQQEGFKMTY DQLYNGENAL
     KNAVVNFSGY CSGVVVSPDG LVFTNHHCGF EAIRSHSTVE HDYMLNGFYA KSFEEELPNE
     DMFVSFMIDQ KDVTDRLTAL GIDNMNSNDQ ANLIDSLQNA LTDSIKKVDS TLHIDIDAFY
     EGNKYYATTY QDFTDLRLVF TVPKSMGKFG GETDNWMWPR QTCDFSVFRI YADPKTNGPA
     AYSKDNVPYH PKRWAQVSMQ GYKEGDYAMT IGYPGSTSRY LSSFGIHEMR DAQNAPRAQV
     RGVKQDVMIR HMRANEAVRI KYDSKYAQSS NYWKNSLGMN KCIDSIGIIN LKRDYEKRIK
     AYQDSTGYLK GQLDFDKMKQ LYDKRFEYMK VWTNYSEAFR RTNEFTTRAM ALDRMEVKGP
     KNKKSKQYIE FADNSEEWDE ALDKEVLAVL MKNYREHVDS KYLPKFYATI DSKFGGDYAK
     YVDYLYANSF LMKSGKPIYI NRKSYLKDPG VQLGLDLLEV LGVLRENINS VSDDINKQEK
     YLCAAKLRME EDLPHYSDAN FTMRLSYGQI GGFDLGGKPS GYYTTAESIV EKMDKGNKII
     DYQVEPIMHK LFSSNNFGKY VDQTTGKFQL CFLTNNDITG GNSGSPMFDG NGNLIGLAFD
     GNWDSLSSDI NFDSHLARCI GVDIRYVLYM MDSWGHADRL LKEINAK
//
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