ID   A0A246J0Y3_9BURK        Unreviewed;       554 AA.
AC   A0A246J0Y3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:OWQ86261.1};
GN   Name=dacB {ECO:0000313|EMBL:OWQ86261.1};
GN   ORFNames=CDN99_20725 {ECO:0000313|EMBL:OWQ86261.1};
OS   Roseateles aquatilis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=431061 {ECO:0000313|EMBL:OWQ86261.1, ECO:0000313|Proteomes:UP000197468};
RN   [1] {ECO:0000313|EMBL:OWQ86261.1, ECO:0000313|Proteomes:UP000197468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 48205 {ECO:0000313|EMBL:OWQ86261.1,
RC   ECO:0000313|Proteomes:UP000197468};
RX   PubMed=18175673; DOI=10.1099/ijs.0.65169-0;
RA   Gomila M., Bowien B., Falsen E., Moore E.R., Lalucat J.;
RT   "Description of Roseateles aquatilis sp. nov. and Roseateles terrae sp.
RT   nov., in the class Betaproteobacteria, and emended description of the genus
RT   Roseateles.";
RL   Int. J. Syst. Evol. Microbiol. 58:6-11(2008).
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:OWQ86261.1}.
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DR   EMBL; NIOF01000011; OWQ86261.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A246J0Y3; -.
DR   Proteomes; UP000197468; 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; 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:OWQ86261.1};
KW   Hydrolase {ECO:0000313|EMBL:OWQ86261.1};
KW   Protease {ECO:0000313|EMBL:OWQ86261.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197468}.
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   554 AA;  59114 MW;  B559255D5B73AEF4 CRC64;
     MEDGRVGRGR RAGPRRARHD RAGAAEGARR AAGRRPCAGG AGHRRLQERR HRAGGHRAGR
     DGALRRSGGT GRVGAAIVSR RLTAALGFVA LAALSGCATV GQPPEPVEAA LRQAGVPPTS
     LAVVAFPVDA PETGLRLNAD RPMAPASTMK AITAVVALDR LGPNSRGQTQ LLAVGEIRDG
     RLEAPLVLKG GGDADLDWGA LWMMLREVRE RHGVRELAGG IVVDRGLFNP ARPEIGAPRF
     DEQAEFPYNV IPDALHLNGN LLQYDFAADD RGLTVRPFPQ FGALAIDTSE VRLNDKPCKD
     WDGGWLPSRF EALPDGAARL VLAGEFPRGC QVLQSLNVLD RQWETAQALR QLWGSLGGTL
     SGEIREGVAP EGARVLAMHR DRPLAELLRP VMKSSDNALA RLIFLRLGAS AAQPGEDTRL
     AADRVVREWF AARKIDTTGL ALENGSGLSR TERATVAQMA AMLAASARGP HGPELLATLP
     VAGVDGTLSR RMKGTAAEGR ARMKTGTLRD VVALAGFVPD SRGRNWIVVA IINDDQAMKA
     RAAIDALVDW VARR
//