ID   PEPDB_STRP6             Reviewed;         499 AA.
AC   Q5X9M0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Probable dipeptidase B;
DE            EC=3.4.13.19;
GN   Name=pepDB; OrderedLocusNames=M6_Spy1758;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT87893.1; Type=Frameshift; Evidence={ECO:0000305};
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; CP000003; AAT87893.1; ALT_FRAME; Genomic_DNA.
DR   MEROPS; C69.002; -.
DR   EnsemblBacteria; AAT87893; AAT87893; M6_Spy1758.
DR   KEGG; spa:M6_Spy1758; -.
DR   HOGENOM; CLU_014823_4_2_9; -.
DR   Proteomes; UP000001167; 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.
FT   CHAIN           1..499
FT                   /note="Probable dipeptidase B"
FT                   /id="PRO_0000220392"
FT   ACT_SITE        26
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   499 AA;  55438 MW;  6D66DBDDFAE95858 CRC64;
     MINKKISLGV LSILTAFSLQ SVSYACTGFI IGKDLTKDGS LLXGRTEDLE PHHNKNFIVR
     LAKDNPAGEK WKDLSNGFEY PLPEHSYRYS AIPDVTPNKG VYDEAGFNEC GVSMSATVSA
     SANDAIQKID PYVKNGLAES SMASVILPSV KTAREGVALI AKIVTEKGAA EGNIVTLADK
     DGIWYMEILS GHQYVAIKFP DDKYAVFPNT FYLGHVDFND KENTIASEDV EKVAKKAKSY
     IEVDGKFHIA KSYNPPLNDA NRSRSFSGIK SLDPDSKVTY KDSNYELLQS TDKTFSLEDA
     MKLQRNRFEG LDLKPLDQMA LDGKGKPKSK KAVKGYAYPI SNPNVMEAHI FQLKKDIPAE
     LGGGVMWLSI GSPRNAPYLP YLGNISRTYE AYQEKSTQYN DKSWYWTVSH INDLVAAHPK
     PFGTKVIDEI KGLEKTWIAE QDKTTKEISD LVVSDPKAAQ EKADKISLDR AEKTFKRLKA
     IEAKLVKEKP KNKKGLNRS