ID   Q5XCB3_STRP6            Unreviewed;       415 AA.
AC   Q5XCB3;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   11-DEC-2019, entry version 80.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:AAT86950.1};
DE            EC=3.4.16.4 {ECO:0000313|EMBL:AAT86950.1};
GN   OrderedLocusNames=M6_Spy0815 {ECO:0000313|EMBL:AAT86950.1};
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636 {ECO:0000313|EMBL:AAT86950.1, ECO:0000313|Proteomes:UP000001167};
RN   [1] {ECO:0000313|EMBL:AAT86950.1, ECO:0000313|Proteomes:UP000001167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394 {ECO:0000313|Proteomes:UP000001167};
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   -!- SIMILARITY: Belongs to the peptidase S11 family.
CC       {ECO:0000256|RuleBase:RU004016}.
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DR   EMBL; CP000003; AAT86950.1; -; Genomic_DNA.
DR   MEROPS; S11.006; -.
DR   EnsemblBacteria; AAT86950; AAT86950; M6_Spy0815.
DR   KEGG; spa:M6_Spy0815; -.
DR   HOGENOM; HOG000086625; -.
DR   KO; K07258; -.
DR   OMA; QNTHFQT; -.
DR   Proteomes; UP000001167; Chromosome.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.410.10; -; 1.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR   InterPro; IPR018044; Peptidase_S11.
DR   InterPro; IPR012907; Peptidase_S11_C.
DR   InterPro; IPR037167; Peptidase_S11_C_sf.
DR   InterPro; IPR001967; Peptidase_S11_N.
DR   Pfam; PF07943; PBP5_C; 1.
DR   Pfam; PF00768; Peptidase_S11; 1.
DR   PRINTS; PR00725; DADACBPTASE1.
DR   SMART; SM00936; PBP5_C; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   SUPFAM; SSF69189; SSF69189; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:AAT86950.1};
KW   Hydrolase {ECO:0000313|EMBL:AAT86950.1};
KW   Protease {ECO:0000313|EMBL:AAT86950.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..415
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004264283"
FT   DOMAIN          299..399
FT                   /note="PBP5_C"
FT                   /evidence="ECO:0000259|SMART:SM00936"
SQ   SEQUENCE   415 AA;  45862 MW;  A1C5E53575B8B722 CRC64;
     MKDIMIKRWA ILFFVVLTCS GLSKIVLAAD FQVGAEHAIV VEADSGRVLY EKDAKTPDAI
     ASLTKLVTAY LVLDKVKSGQ LQLSDQVNLS DYAFELTKDR SLSNVPFDKK TYSVQDLLTA
     TLVASSNSAA IALAEKVAGS EPHFVNQMRE QLSHWGITSG KILNASGLPN EVLKDHRYPG
     SALEEENTLS AQDVAVVTMR LLEDFPEILE ITKQTEVNFA GNSIKSFNQL LPGMAKGRAG
     VDGLKTGTTD LAGHCLVVTS IENGMRVITV ILNADGSDKN QNTRFEQANR LLDYVARTYC
     RRKILKKGSL VSERSLPIQD GQVKELPVSV AEDVTIILQQ GEQVPKPKQF MISETSLLAP
     ITKGEVVAYL TSPRITDQSV RYLKEPKRIP LKASQSLKKA SDLQLWWRDF LEKRR
//