ID   A0A0K0G715_9FIRM        Unreviewed;       476 AA.
AC   A0A0K0G715;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KKE78313.1};
GN   ORFNames=WH51_13430 {ECO:0000313|EMBL:KKE78313.1};
OS   Bacilli bacterium VT-13-104.
OC   Bacteria; Bacillota; Bacilli.
OX   NCBI_TaxID=1637974 {ECO:0000313|EMBL:KKE78313.1, ECO:0000313|Proteomes:UP000034981};
RN   [1] {ECO:0000313|Proteomes:UP000034981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VT-13-104 {ECO:0000313|Proteomes:UP000034981};
RA   Tetz V., Tetz G.;
RT   "Bacilli bacterium VT-13-104.";
RL   Submitted (APR-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:KKE78313.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LAZH01000052; KKE78313.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K0G715; -.
DR   PATRIC; fig|1637974.4.peg.2834; -.
DR   Proteomes; UP000034981; 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:KKE78313.1};
KW   Hydrolase {ECO:0000313|EMBL:KKE78313.1};
KW   Protease {ECO:0000313|EMBL:KKE78313.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034981}.
SQ   SEQUENCE   476 AA;  52562 MW;  BA3E77172818F3B9 CRC64;
     MELIHASESI TSEINPSWSL EEKINKIFED ERLQGSITGI SVRKADTGEE IYSHHGNIRL
     HPASNMKILT ASTALEVLGP DHKFKTKVYT DGELVGGVLK GNLYIQGGGD PTLLKEDIDE
     LVNHLKKLEV RKVEGDLVAD DTWYDNIRLS QDLNWSDEPF HTGAQISALT LSPDKGYDAG
     TVMLEIIPGK RQGDVAQVNV IPETDYVKIL NQTRTVHKDE KKQLTIDRVH GENTIIVEGD
     IPIGASKEKT WAAVWDPTSY VLNIFASSLI SNGISFSSEL EQRLDAVPKD ATLLAENQSM
     PLKELLLPFM KLSNNTIGEV LVKEMGKAVH GEGSWEKGLA VMEESIINLG MDPNLFLLRD
     GSGMSHKNFV SSSELTKLLY EIQQKDWFTV FENSLPVAGE SEKLVGGTLR SRMDNLKGNV
     RAKTGSITGV QTLSGYVTNI NGEKLIFSIL NNNYIEDSMS AIQDTMVTIL ATHNLN
//