ID A0A1P8RW54_9FLAO Unreviewed; 695 AA.
AC A0A1P8RW54;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=BWZ20_07570 {ECO:0000313|EMBL:APY08166.1};
OS Winogradskyella sp. J14-2.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=1936080 {ECO:0000313|EMBL:APY08166.1, ECO:0000313|Proteomes:UP000187462};
RN [1] {ECO:0000313|EMBL:APY08166.1, ECO:0000313|Proteomes:UP000187462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J14-2 {ECO:0000313|EMBL:APY08166.1,
RC ECO:0000313|Proteomes:UP000187462};
RA Kim J.H., Chi W.-J.;
RT "Genome sequence of Winogradskyella sp. J14-2 isolated from seawater in
RT Jeju island.";
RL Submitted (JAN-2017) 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}.
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DR EMBL; CP019388; APY08166.1; -; Genomic_DNA.
DR RefSeq; WP_076618469.1; NZ_CP019388.1.
DR AlphaFoldDB; A0A1P8RW54; -.
DR STRING; 1936080.BWZ20_07570; -.
DR KEGG; wij:BWZ20_07570; -.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000187462; Chromosome.
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; 2.
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, ECO:0000313|EMBL:APY08166.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187462};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU366067}; Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 18..695
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023040652"
SQ SEQUENCE 695 AA; 78736 MW; EBDC0BD06CA4D963 CRC64;
MRFIKLLCFF VVFQVSAQQG GMWIPSLLEG MNEDEMQSLG SKLTAKDIYD VNNSSLKDAI
GHFNGGCTSE VISDKGLVLT NHHCGFSQIQ SHSSLENDYI KNGFWAMSLE EELPNEGLFI
EFIVSIHDVT DTVLNGVNET MTEKEKQSLI TRNSNAAMAS WPKEKWQDVK TKSFYEGNQY
FLFVTERFED IRLVGAPPSS IGKFGSDTDN WVFPRHTGDF SMFRIYADKN NRPAKYSKDN
VPYKPKHYLP VSLDGVEEGD FTMVFGFPGR TNEYLPAVAI EHITKEFNPT NIEIREAALK
VIDANMKASD EVRIKYASKQ ARIANAWKKW IGENLGIEKS DAVAKRREFE ATFKKALKEN
GLEAKYGHIL PEFDKLYKEF GPINIKRRNF VEVFLVTSEL MQITFRAYQV EQALLANPES
LERAKASLKG RFEGILKNFD ANVDKGVYLN VMPLYGKPVD ASIYDKTAFT DLDSALKLLE
GDAKTVIKNL NNDAAYAYAK PIIDEFFTTI DAEFQQKNES ISALQTEYMT ALMKALPNER
YFPDANSTLR VTYGQVRGYS PRDAVYYEPV SHLKGVMEKY VPGDYEFDVP QKLIDLYEAK
DYGQYADSNG DMPVCFLGTN HTTGGNSGSP AIDAEGNLVG LNFDRVWEGT MSDMNYDPEI
CRNIMVDLRY VLFIVDKYAG AKHLIDEMKL VHPKK
//
