ID   DPP11_SHEPC             Reviewed;         732 AA.
AC   A4Y3F4;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Asp/Glu-specific dipeptidyl-peptidase {ECO:0000303|PubMed:23246913};
DE            EC=3.4.14.- {ECO:0000269|PubMed:23246913};
DE   AltName: Full=Dipeptidyl-peptidase 11 {ECO:0000303|PubMed:23246913};
DE            Short=DPP11 {ECO:0000303|PubMed:23246913};
DE   Flags: Precursor;
GN   Name=dpp11; OrderedLocusNames=Sputcn32_0757 {ECO:0000312|EMBL:ABP74487.1};
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 / ATCC BAA-453;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF
RP   SER-684 AND LYS-691.
RC   STRAIN=ATCC 8071 / JCM 20190;
RX   PubMed=23246913; DOI=10.1016/j.biochi.2012.11.019;
RA   Rouf S.M., Ohara-Nemoto Y., Hoshino T., Fujiwara T., Ono T., Nemoto T.K.;
RT   "Discrimination based on Gly and Arg/Ser at position 673 between
RT   dipeptidyl-peptidase (DPP) 7 and DPP11, widely distributed DPPs in
RT   pathogenic and environmental gram-negative bacteria.";
RL   Biochimie 95:824-832(2013).
CC   -!- FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of
CC       oligopeptides. Shows a strict specificity for acidic residues (Asp or
CC       Glu) in the P1 position, and has probably a hydrophobic residue
CC       preference at the P2 position. Preferentially cleaves the synthetic
CC       substrate Leu-Glu-methylcoumaryl-7-amide (Leu-Glu-MCA) as compared to
CC       Leu-Asp-MCA. {ECO:0000269|PubMed:23246913}.
CC   -!- SIMILARITY: Belongs to the peptidase S46 family. {ECO:0000305}.
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DR   EMBL; CP000681; ABP74487.1; -; Genomic_DNA.
DR   RefSeq; WP_011918692.1; NC_009438.1.
DR   AlphaFoldDB; A4Y3F4; -.
DR   SMR; A4Y3F4; -.
DR   STRING; 319224.Sputcn32_0757; -.
DR   MEROPS; S46.003; -.
DR   GeneID; 45041191; -.
DR   KEGG; spc:Sputcn32_0757; -.
DR   eggNOG; COG3591; Bacteria.
DR   eggNOG; COG4990; Bacteria.
DR   HOGENOM; CLU_013776_0_0_6; -.
DR   OMA; KDWFFNP; -.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB.
DR   GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:InterPro.
DR   GO; GO:0043171; P:peptide catabolic process; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR019500; Pep_S46.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR000126; V8_ser_AS.
DR   PANTHER; PTHR38469; PTHR38469; 1.
DR   Pfam; PF10459; Peptidase_S46; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS00673; V8_SER; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Hydrolase; Protease; Serine protease; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..732
FT                   /note="Asp/Glu-specific dipeptidyl-peptidase"
FT                   /id="PRO_5002676185"
FT   ACT_SITE        80
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:V5YM14"
FT   ACT_SITE        215
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:V5YM14"
FT   ACT_SITE        666
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:V5YM14"
FT   MUTAGEN         684
FT                   /note="S->R: Catalytic activity highly decreases and the
FT                   Asp/Glu preference is inverted, i.e., peptidase activity
FT                   toward Leu-Glu-MCA becomes smaller than that to Leu-Asp-
FT                   MCA. Partial restoration of activity for Leu-Asp-MCA; when
FT                   associated with G-691."
FT                   /evidence="ECO:0000269|PubMed:23246913"
FT   MUTAGEN         691
FT                   /note="K->G: Disrupts the acidic residue specificity, as it
FT                   more efficiently degrades Ala-Asn- and Leu-Gln-MCA. Partial
FT                   restoration of activity for Leu-Asp-MCA; when associated
FT                   with R-684."
FT                   /evidence="ECO:0000269|PubMed:23246913"
SQ   SEQUENCE   732 AA;  82383 MW;  8542F88B2FF06B58 CRC64;
     MRIALVATLV LTSGIANADE GQWQPYQMPS IADKLSERGI DIPAEKLADL TSYPMNAVVG
     LGYCTASFVS PQGLVVTNHH CAYKAIQYNT KQEHNYLEQG FLATSMDKEP SAGPNERLYI
     TEAVTDVTKD VTKELSQDPL TRYEEIQNNS KALIKNCEVD DNYRCNVRSF HNGLEYYLIK
     QLMIRDVRLV YAPPESVGGY GGDIDNYEYP RHSGDFAFLR AYVGKDGKPA AYAEDNIPYK
     PKSYLKVNAD GVKAGDGVFV AGYPGTTSRY NLTSELKFAS DWLYPTQAKR YQLQIDTINA
     MGQEDADIAI KYAGNMASMA NRMKKLNGLL AGFKATDIIG IKQSREDNFL AWLKQNPKLN
     QNLIAELEVL LAEQQQVFQS NYYFTNAQSS TLLTAANSLY RLAKEKQKSD AEREIGYQER
     DLAMFSSRLK RIDSSFHVDV DKTLWQQDLR AYLAQPNRIA ALDDALDLNN KETNLEAKLD
     GLYSLTTLTD QAQRLAWMDA DTTTFETSTD PFIRLAVALY DTNMAQEKAE KILDGKLSTA
     RPDYMAAVIE YYKANNWPVY PDANGTLRIS YGMVDGYQSR DALYKQPFTR LDGIVAKHTG
     AEPYNAPQKL LDAISEQRFG DHLVKSVYQD PRGWICRLFS CLDKPEEFNS VPVNFLSSVD
     TTGGNSGSPV FNGKGELVGL NFDSTYEAIT KDWFFNPTIT RAVHVDIRYI LWMMDKVDHA
     DNLIKELDLV RN