ID S0GNQ0_9BACT Unreviewed; 719 AA.
AC S0GNQ0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, 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=C803_02871 {ECO:0000313|EMBL:EOS17237.1};
OS Parabacteroides goldsteinii dnLKV18.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=1235789 {ECO:0000313|EMBL:EOS17237.1, ECO:0000313|Proteomes:UP000014140};
RN [1] {ECO:0000313|EMBL:EOS17237.1, ECO:0000313|Proteomes:UP000014140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=dnLKV18 {ECO:0000313|Proteomes:UP000014140};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Kuhn K., Stappenbeck T., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Parabacteroides goldsteinii dnLKV18.";
RL Submitted (APR-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:EOS17237.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ASSQ01000014; EOS17237.1; -; Genomic_DNA.
DR RefSeq; WP_010802002.1; NZ_KE159519.1.
DR AlphaFoldDB; S0GNQ0; -.
DR PATRIC; fig|1235789.3.peg.2869; -.
DR HOGENOM; CLU_013776_0_0_10; -.
DR Proteomes; UP000014140; 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 Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU366067}; 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_5023152896"
SQ SEQUENCE 719 AA; 81920 MW; B2D307967EF36930 CRC64;
MKKILLSVLA AALSLPAVAD EGMWLLPLLQ QQKFPEMQAL GLKLQDYDIY SPDSASLKDA
VVIFGGGCTG EIVSPDGLLL TNHHCGYGQI QQHSTLEHDY LTDGFWATTR EQELPNPGLT
VTFIDKIEDV TDYVKKELEK DTDPQSMNFL SPKYLNGLAK AKVGEKFLQD NPGTEVEIKA
FYGGNVYYMF TKKIYSDIRL VGAPPSSVGK FGADTDNWMW PRHTGDFSVF RVYADANGNP
AEYSESNVPL RPKRWFKISV KGVEEDDYAM MMGFPGRTNK YYTSWEVAER RDIDNTVRIN
IRNLRQEVML DEMLKDPSVR IQYASKYAGS TNAYKNAIGS NWAIKKRNFE QVKKEEQDRL
IAWAQKNNES SYPEALLTLE QIVSDRKDLR FRSWMLDEAI LRGIEFTKVP TEVQSVSDAL
KGKDRNEQQK QIRLLDMAYH RFADKDYAPE VDKKIAKVML KEYRRLVPAK SQPAYFSLID
KKFKGDVDRF VDYLFDKSIY GSEENFDKFK TRPSVKALEQ DPMILFAKSV QEEKANLNAA
LADFDSGYAL AHKEYVKGLL AMYQDKANFP DANFSLRLTY GQVKGYRPKD AVYYNCQTTL
DGVMEKEDST NWEFVVPSRL KALYEAKDFG RYQMPDGRMP VAFSATTHTT GGNSGSPVLN
ANGELIGINF DRNWEGVGGD IQYLPDYQRS IIVDIRYVLF LIDKYAGAGY LLEEMDLVE
//