ID   A0A0N0B2D3_9ACTN        Unreviewed;       461 AA.
AC   A0A0N0B2D3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KOX47670.1};
GN   ORFNames=ADL09_13405 {ECO:0000313|EMBL:KOX47670.1};
OS   Streptomyces sp. NRRL F-7442.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519498 {ECO:0000313|EMBL:KOX47670.1, ECO:0000313|Proteomes:UP000037772};
RN   [1] {ECO:0000313|EMBL:KOX47670.1, ECO:0000313|Proteomes:UP000037772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-7442 {ECO:0000313|EMBL:KOX47670.1,
RC   ECO:0000313|Proteomes:UP000037772};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOX47670.1}.
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DR   EMBL; LGEH01000139; KOX47670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0B2D3; -.
DR   PATRIC; fig|1519498.3.peg.2782; -.
DR   Proteomes; UP000037772; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000667; Peptidase_S13.
DR   NCBIfam; TIGR00666; PBP4; 1.
DR   PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR   Pfam; PF02113; Peptidase_S13; 2.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:KOX47670.1};
KW   Hydrolase {ECO:0000313|EMBL:KOX47670.1};
KW   Protease {ECO:0000313|EMBL:KOX47670.1}.
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   461 AA;  46363 MW;  3F617718EADE3710 CRC64;
     MAAGVVTAAG PWDSTGQRTA ERDRAVALEH TGGADHGRGP GASGTASGSP RPAPSAGPVL
     TGLGGATTPG GVKAAPGTEN LADLLDPLLK DDPALGERRA AAVVDLTTGK RLYGLDADAA
     LVPASTTKIA TAVAALTALG PDHRLTTRTA LEADTGELVL VGGGDPTLTA REDARGLAGL
     RTLAEQTAAA LKKRDVRKVT LSYDTTLYAG PELHPIGVNE NLAPVTALMA DEGRTDDSTS
     GPAPRVPDPA ADAARTFADL LKQHGVTASP PGPSKATGRA TTLAAVSSPP LSALVERMLT
     NSDNDLAEAL ARHTAVATGR RADFAGAGAA VAARLEQLGL PVRGARFHDG SGLDRTDLIT
     PGLLTALLTE AAAPDRPQLR PVLTGLPVAH FTGTLAARYT DGAAGLVRAK TGTLTGVNTL
     AGTVTTPDGR LLAFAFLTNA TTDAWAAQSA LDRAATGLTS P
//