ID   A0A160DUD2_9GAMM        Unreviewed;       510 AA.
AC   A0A160DUD2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:ANB17854.1};
GN   ORFNames=I596_1831 {ECO:0000313|EMBL:ANB17854.1};
OS   Dokdonella koreensis DS-123.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dokdonella.
OX   NCBI_TaxID=1300342 {ECO:0000313|EMBL:ANB17854.1, ECO:0000313|Proteomes:UP000076830};
RN   [1] {ECO:0000313|EMBL:ANB17854.1, ECO:0000313|Proteomes:UP000076830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-123 {ECO:0000313|EMBL:ANB17854.1,
RC   ECO:0000313|Proteomes:UP000076830};
RA   Kim J.F., Lee H., Kwak M.-J.;
RT   "Complete genome sequence of Dokdonella koreensis DS-123T.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
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DR   EMBL; CP015249; ANB17854.1; -; Genomic_DNA.
DR   RefSeq; WP_067646410.1; NZ_CP015249.1.
DR   AlphaFoldDB; A0A160DUD2; -.
DR   STRING; 1300342.I596_1831; -.
DR   KEGG; dko:I596_1831; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000076830; Chromosome.
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; 1.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:ANB17854.1};
KW   Hydrolase {ECO:0000313|EMBL:ANB17854.1};
KW   Protease {ECO:0000313|EMBL:ANB17854.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076830};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..510
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007813849"
SQ   SEQUENCE   510 AA;  53429 MW;  ADCCBA6E102D7C90 CRC64;
     MKRPACWLAA LLLGTAGGTV QAAGAAATRA QIDAILAEPR FAAASWGVQA VSIDSGRTVY
     AHQAERLLVP ASTAKLYTAA LALATFGGDY RIPTTLFATA APARDGELHG DLVLYGYGDP
     ALGADADVSW ADRLAIALRR RGVTRVHGDL IGDATRFAAP LFGAGWEAAD LQSWFGMPAA
     ALSVDENLVT VRIRPAPQVG AMAGLRFEPP GSAPDLANRL LTVARGRPTD VGLFRAPGQA
     TLQAFGSIAA DAGEQRYRLA LVDPALTAAG QLRDALARQG VTLEGRLRSV YWPERTVAMA
     ADAPQRIAEV HSPPLADLVR RGLKVSQNLY LQNLFLLVGA AEADKVRALQ PDSLPFRSTD
     QRAADALRRY LSGLGITPQQ ASIEDGAGLS RRNLTSAAAL ATLLQRWGDT PDGAAFRLAL
     PQAGVDGSLA GRLRDTPAQG RVHAKTGAMN GIRGLAGYLT TAAGERLAFA ILLNNYQPPG
     DAATARPSGE IDRIVLALAA LDERSSAARP
//