ID   DACA_GEOSE              Reviewed;         452 AA.
AC   Q05523;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=D-alanyl-D-alanine carboxypeptidase DacA;
DE            Short=CPase;
DE            Short=DD-carboxypeptidase;
DE            Short=DD-peptidase;
DE            EC=3.4.16.4;
DE   AltName: Full=Penicillin-binding protein 5;
DE            Short=PBP-5;
DE   Flags: Precursor;
GN   Name=dacA;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8370539; DOI=10.1016/0378-1119(93)90666-q;
RA   Despreaux C.W., Manning R.F.;
RT   "The dacA gene of Bacillus stearothermophilus coding for D-alanine
RT   carboxypeptidase: cloning, structure and expression in Escherichia coli and
RT   Pichia pastoris.";
RL   Gene 131:35-41(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 422-452.
RX   PubMed=6780559; DOI=10.1016/s0021-9258(19)69916-3;
RA   Waxman D.J., Strominger J.L.;
RT   "Primary structure of the COOH-terminal membranous segment of a penicillin-
RT   sensitive enzyme purified from two Bacilli.";
RL   J. Biol. Chem. 256:2067-2077(1981).
RN   [3]
RP   ACTIVE SITE SER-66.
RX   PubMed=111240; DOI=10.1073/pnas.76.6.2730;
RA   Yocum R.R., Waxman D.J., Rasmussen J.R., Strominger J.L.;
RT   "Mechanism of penicillin action: penicillin and substrate bind covalently
RT   to the same active site serine in two bacterial D-alanine
RT   carboxypeptidases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 76:2730-2734(1979).
CC   -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC       wall precursors.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall.
CC   -!- SIMILARITY: Belongs to the peptidase S11 family. {ECO:0000305}.
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DR   EMBL; X68587; CAA48577.1; -; Genomic_DNA.
DR   PIR; JN0801; JN0801.
DR   AlphaFoldDB; Q05523; -.
DR   SMR; Q05523; -.
DR   ChEMBL; CHEMBL3271926; -.
DR   MEROPS; S11.001; -.
DR   SABIO-RK; Q05523; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.410.10; -; 1.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR   InterPro; IPR018044; Peptidase_S11.
DR   InterPro; IPR012907; Peptidase_S11_C.
DR   InterPro; IPR037167; Peptidase_S11_C_sf.
DR   InterPro; IPR001967; Peptidase_S11_N.
DR   Pfam; PF07943; PBP5_C; 1.
DR   Pfam; PF00768; Peptidase_S11; 1.
DR   PRINTS; PR00725; DADACBPTASE1.
DR   SMART; SM00936; PBP5_C; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   SUPFAM; SSF69189; SSF69189; 1.
PE   1: Evidence at protein level;
KW   Carboxypeptidase; Cell shape; Cell wall; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Hydrolase; Peptidoglycan synthesis; Protease;
KW   Secreted; Signal; Sporulation.
FT   SIGNAL          1..30
FT   CHAIN           31..452
FT                   /note="D-alanyl-D-alanine carboxypeptidase DacA"
FT                   /id="PRO_0000027227"
FT   ACT_SITE        66
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000269|PubMed:111240"
FT   ACT_SITE        69
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   452 AA;  51002 MW;  6765493B54D7E87E CRC64;
     MRRRKQNWLF WLLSICLCLT FGPFQQTVKA ESAPLDIRAD AAILVDAQTG RILYEKNIDT
     VLGIASMTKM MTEYLLLDAI KAKRVKWDQM YTPSDYVYRL SQDRALSNVP LRKDGKYTVR
     ELYEAMAIYS ANGATVAIAE IIAGSEKNFV KMMNDKAKEL GLKDYKFVNA TGLSNKDLKG
     FHPEGTSTNE ENVMSARAMA MLAYRLLKDH PEVLKTASIP HKVFREGTKD EIKMDNWNWM
     LPGLVYGYEG VDGLKTGYTE FAGNCFTGTA KRNGVRLISV VMNAKDASGK TTKEARFKET
     EKLFNYGFNQ YSLETLYPKG YQLKGKETLP VVKGKEKEVR VATGKNLDLL VKNGEEKQYK
     PVYVLDKKKM TKEGKLVAPL KKGETVGYMT LEYKGDDSLA FLSPDMQKNI RVPLVTTAEV
     EKANWFVLSM RAVGGLFVDL WTSVAKTVKG WL