ID   A0A291GC14_9RHOB        Unreviewed;       499 AA.
AC   A0A291GC14;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:ATG47688.1};
GN   Name=dacB {ECO:0000313|EMBL:ATG47688.1};
GN   ORFNames=CEW89_08955 {ECO:0000313|EMBL:ATG47688.1};
OS   Celeribacter ethanolicus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1758178 {ECO:0000313|EMBL:ATG47688.1, ECO:0000313|Proteomes:UP000217935};
RN   [1] {ECO:0000313|EMBL:ATG47688.1, ECO:0000313|Proteomes:UP000217935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSPH2 {ECO:0000313|EMBL:ATG47688.1,
RC   ECO:0000313|Proteomes:UP000217935};
RA   Woo J.-H., Kim H.-S.;
RT   "Celeribacter sp. TSPH2 complete genome sequence.";
RL   Submitted (JUN-2017) 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; CP022196; ATG47688.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291GC14; -.
DR   STRING; 1758178.GCA_001550095_01308; -.
DR   KEGG; ceh:CEW89_08955; -.
DR   OrthoDB; 5372081at2; -.
DR   Proteomes; UP000217935; 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; 1.
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:ATG47688.1};
KW   Hydrolase {ECO:0000313|EMBL:ATG47688.1};
KW   Protease {ECO:0000313|EMBL:ATG47688.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217935};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..499
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012561487"
SQ   SEQUENCE   499 AA;  52071 MW;  7F3CC08BF03D67D1 CRC64;
     MNRRKALGLL LGGAAQVVAQ AAGAEGLVAS AIPKPRPADL YRRSIPTGEA LIAAAGLSGE
     VSYAVAGSAT GDLHEVHEPL LRLPPASVAK TVTALYALHH LGAEHRFVTR VLASGPVVNG
     VVQGDLVLVG GGDPTLDTDG LGVLAGKLCE AGVTGVKGQF YVDDTALPRI AQIDGEQVEY
     AGYNPTISGL NLNYNRVHFE WKRQGEDYNL KMDARAERYA PDVRIARISV AARDLPVFDH
     VAGQGRDEWT VARGALGNGG ARWLPVRLPG LYAAEVFQAV ANAQGVRLPQ GQRGTVNGMG
     SGTELARIES APLSVVVRDM LKYSTNLTAE AIGLTASKAR GLAPATLAGS AMAMSEWAQS
     ALGMRHVALV DHSGLGGASK VTTVDMVHML SAPGVEATLA PLMKPIPMRD AKGNVIQNSP
     VSVHAKTGTL DFVSALAGYV DAPGGARMAF AIFAADVPRR EAAKAAGAEE RPQGARTFNT
     RAKKLQQALI ERWAGVYAG
//