ID   PEPDB_STRP1             Reviewed;         498 AA.
AC   Q99XS1; Q48W99;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Probable dipeptidase B;
DE            EC=3.4.13.19;
GN   Name=pepDB; OrderedLocusNames=SPy_2066, M5005_Spy1758;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid;
CC         Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC         ChEBI:CHEBI:77460; EC=3.4.13.19;
CC   -!- SIMILARITY: Belongs to the peptidase C69 family. {ECO:0000305}.
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DR   EMBL; AE004092; AAK34726.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ52376.1; -; Genomic_DNA.
DR   RefSeq; NP_270005.1; NC_002737.2.
DR   AlphaFoldDB; Q99XS1; -.
DR   SMR; Q99XS1; -.
DR   STRING; 1314.HKU360_01872; -.
DR   MEROPS; C69.002; -.
DR   PaxDb; Q99XS1; -.
DR   EnsemblBacteria; AAK34726; AAK34726; SPy_2066.
DR   KEGG; spy:SPy_2066; -.
DR   KEGG; spz:M5005_Spy1758; -.
DR   PATRIC; fig|160490.10.peg.1792; -.
DR   HOGENOM; CLU_014823_0_1_9; -.
DR   OMA; DKFAVFP; -.
DR   Proteomes; UP000000750; Chromosome.
DR   GO; GO:0070004; F:cysteine-type exopeptidase activity; IEA:InterPro.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR005322; Peptidase_C69.
DR   PANTHER; PTHR12994; PTHR12994; 1.
DR   Pfam; PF03577; Peptidase_C69; 1.
PE   3: Inferred from homology;
KW   Dipeptidase; Hydrolase; Protease; Reference proteome.
FT   CHAIN           1..498
FT                   /note="Probable dipeptidase B"
FT                   /id="PRO_0000220390"
FT   ACT_SITE        26
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   498 AA;  55499 MW;  B9394DC94C19AE4D CRC64;
     MINKKISLGV LSILTAFSLQ SVSYACTGFI IGKDLTKDGS LLYGRTEDLE PHHNKNFIVR
     LAKDNPAGEK WKDLSNGFEY PLPEHSYRYS AIPDVTPNKG VYDEAGFNEF GVSMSATVSA
     SANDAIQKID PYVKNGLAES SMTSVILPSV KTAREGVALI AKIVTEKGAA EGNIVTLADK
     DGIWYMEILS GHQYVAIKFP DDKYAVFPNT FYLGHVDFND KENTIASEDV EKVAKKAKSY
     TEVDGKFHIA KSYNPPLNDA NRSRSFSGIK SLDPDSKVTY KDSNYELLQS TDKTFSLEDA
     MKLQRNRFEG LDLKPLDQMA LDGKGKPKSK KAVKGYAYPI SNPNVMEAHI FQLKKDIPAE
     LGGVMWLSIG SPRNAPYLPY LGNISRTYEA YQEKSTQYND KSWYWTVSHI NDLVAAHPKP
     FGTKVIDEMK GLEKTWIAEQ DKSTKEISDL VVSDPKAAQE KADKISLDRA EKTFKRLKAI
     EAKLVKEKPK NKKGLNRS