ID   R5FVE4_9PORP            Unreviewed;       700 AA.
AC   R5FVE4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, 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=BN460_00032 {ECO:0000313|EMBL:CCY08828.1};
OS   Porphyromonas sp. CAG:1061.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas; environmental samples.
OX   NCBI_TaxID=1262916 {ECO:0000313|EMBL:CCY08828.1, ECO:0000313|Proteomes:UP000018064};
RN   [1] {ECO:0000313|EMBL:CCY08828.1, ECO:0000313|Proteomes:UP000018064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:1061 {ECO:0000313|Proteomes:UP000018064};
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:CCY08828.1}.
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DR   EMBL; CAXO010000046; CCY08828.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5FVE4; -.
DR   Proteomes; UP000018064; 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; 2.
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..22
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT   CHAIN           23..700
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5022995253"
SQ   SEQUENCE   700 AA;  79522 MW;  079967D51EBC7D6A CRC64;
     MKQLRLSLAM GLLLLLAPMA KADKGMYLIN SIKQENMDRM RELGLKLSPE ELFSADGNSL
     SSAVAIFDNG CTSITVSNQG LLFTNHHCGY RSIQSQSSVE HDYLRDGFVA HNMAEELPIE
     GLEVKYLREF VDVTDQVTEG TENMTDEMAR IQAIQMASSL LVAKYADDPH TDADIYSFYE
     NNKFYLVVYD VFTDVRMVFA PPTSMGKFGA DTDNWMWPRH TNDFSVFRVY ADKNNKPADY
     SADNKPYQPR HFAKVSIRGI EEGDYAMTIG FPGSTDRYLS SWGVENRIVN ENEPRILVRG
     IKQEIWMKHM NAEQAIRIQY ASKYAGSSNY WKNSIGMNKG LRRLNVVENK RQIERQFSEW
     VAADAARTAK YAGVLDSLRI PLEAMGKLFY NFTILSEAMS GTEFRSFVAM PSPDMAEFDA
     DALYKDFSTK VGRATLPAML RVTKEQVAPE YLPSIFSEIK SKFGGDYEAY AQYVYDNSVV
     LHKDRMVEAL KNYELFAKAH DTDPAVVISN SYRDALMKLY GEINNYQYQY AKGRRLFMAG
     LQEMSDEYLP SDANFTMRLS YGSVGGYRPY DGAYYDYYTT EEGVLEKQDP ESTEFAVQPE
     ILDMMRNKEF GEYAAKDGHL HLCFISNNDI TGGNSGSPVF DGEGNVIGLA FDGNWEAMSG
     DIEFEPNLQR TISVDIRYVL WAIQHWGKAD YLINELTLVK
//