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PEPDA_STRP1
ID   PEPDA_STRP1             Reviewed;         472 AA.
AC   Q9A0M0; Q48ZQ8;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Probable dipeptidase A;
DE            EC=3.4.13.19;
GN   Name=pepDA; Synonyms=pepD; OrderedLocusNames=SPy_0713, M5005_Spy0542;
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; AAK33666.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ51160.1; -; Genomic_DNA.
DR   RefSeq; NP_268945.1; NC_002737.2.
DR   AlphaFoldDB; Q9A0M0; -.
DR   SMR; Q9A0M0; -.
DR   STRING; 1314.HKU360_00552; -.
DR   MEROPS; C69.001; -.
DR   PaxDb; Q9A0M0; -.
DR   PRIDE; Q9A0M0; -.
DR   EnsemblBacteria; AAK33666; AAK33666; SPy_0713.
DR   KEGG; spy:SPy_0713; -.
DR   KEGG; spz:M5005_Spy0542; -.
DR   PATRIC; fig|160490.10.peg.607; -.
DR   HOGENOM; CLU_014823_4_2_9; -.
DR   OMA; DLTYSHE; -.
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..472
FT                   /note="Probable dipeptidase A"
FT                   /id="PRO_0000220386"
FT   ACT_SITE        10
FT                   /evidence="ECO:0000255"
FT   CONFLICT        1..9
FT                   /note="MDKKIQRFS -> MA (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        424
FT                   /note="V -> A (in Ref. 2; AAZ51160)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   472 AA;  53855 MW;  86755CF133A24F95 CRC64;
     MDKKIQRFSC TTILVGKKAS YDGSTMVART EDSQNGDFTP KKMIVVKPED QPRHYRSVQS
     SFEMDLPDNP MTYTSVPDAL GKDGIWAEAG VNEANVAMSA TETITTNSRV LGADPLVASG
     IGEEDMVTLV LPYIRSAREG VLRLGAILED YGTYESNGVA FSDEHDIWWL ETIGGHHWIA
     RRVPDDAYVT NPNQFGIDHF EFNNPEDYLC SADLKDFIDT YHLDLTYSHE HFNPRYAFGS
     QRDKDRQYNT PRAWIMQKFL NPEIVQDPRS FALAWCQKPY RKITVEDVKY VLSSHYQDTG
     YDPYGSEGTP VSKKVFRPIG INRTSQTAIL HIRPNKPQEI AAIQWMAYGS MPFNTMVPFF
     TQVKTIPDYF ANTYENVFTD NFYWTNRLIA ALADPHYNHH ETDLDNYLEE TMAKGHAMLH
     AVEVQLLAGE TVDLEEENQK MSDYVQGETQ TLLNKILFDA SNLMTNRFSL SD
 
 
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