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