ID   A0A0A0BKR6_9CELL        Unreviewed;       477 AA.
AC   A0A0A0BKR6;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KGM09123.1};
GN   ORFNames=N869_08015 {ECO:0000313|EMBL:KGM09123.1};
OS   Cellulomonas bogoriensis 69B4 = DSM 16987.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1386082 {ECO:0000313|EMBL:KGM09123.1, ECO:0000313|Proteomes:UP000054314};
RN   [1] {ECO:0000313|EMBL:KGM09123.1, ECO:0000313|Proteomes:UP000054314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=69B4 {ECO:0000313|EMBL:KGM09123.1,
RC   ECO:0000313|Proteomes:UP000054314};
RA   Chen F., Li Y., Wang G.;
RT   "Genome sequencing of Cellulomonas bogoriensis 69B4.";
RL   Submitted (AUG-2013) 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:KGM09123.1}.
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DR   EMBL; AXCZ01000214; KGM09123.1; -; Genomic_DNA.
DR   RefSeq; WP_052105559.1; NZ_AXCZ01000214.1.
DR   AlphaFoldDB; A0A0A0BKR6; -.
DR   OrthoDB; 56883at2; -.
DR   Proteomes; UP000054314; 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:KGM09123.1};
KW   Hydrolase {ECO:0000313|EMBL:KGM09123.1};
KW   Protease {ECO:0000313|EMBL:KGM09123.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054314}.
SQ   SEQUENCE   477 AA;  48456 MW;  0BF50AEFB1B3742A CRC64;
     MAARTSRRSG PVAAAAAVAL VLGAGGYLVA DAHDVVPGFL TLEPVPPPPS PFPVAPAAQE
     PPPLEIVLPP VDVDVPVPDA QELTALARAA ADHEWMGDSV GIVVADQLTG EVLVDVDGDR
     PRTPASTAKM ATGFAAVRAL GPDARLATTV VQAGSGRLVL VGGGDVMLAQ GAGDPTAVNG
     HAGLADLADQ VVLRLELAGV DEVALDVDDT FFTGPRLAPG WADTDLSGGF VAPVTALMVN
     IAKTREEPYP PRHRDPSLHA AQVLAAALEE RGVTVTGAPT RTEAPEGATV LGMVESATLR
     DVVAYSLQTS DNTVSEALGR VTAHARGLPT SFQGATRAVI AEMTDAGLDT TGAVLADCSG
     LADGSWLPAR LLVDLVVLSA DPTDTATLPV AVDMPVAGWQ GTLAERLTST PARGLVRAKT
     GSLRGVTSLS GTVVTVEGRP LVFAVLADQT PPGGQLGPRR VIDTFVQQLA GCGCGLP
//