ID CBPM_STRAL Reviewed; 255 AA. AC P00733; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 02-SEP-2026, entry version 136. DE RecName: Full=Zinc D-Ala-D-Ala carboxypeptidase; DE EC=3.4.17.14; DE AltName: Full=D-alanyl-D-alanine carboxypeptidase; DE AltName: Full=Metallo DD-peptidase; DE AltName: Full=Zn DD-peptidase; DE Flags: Precursor; OS Streptomyces albus G. OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1962; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=G; RX PubMed=2276609; DOI=10.1016/0378-1097(90)90059-y; RA Duez C., Lakaye B., Houba S., Dusart J., Ghuysen J.-M.; RT "Cloning, nucleotide sequence and amplified expression of the gene encoding RT the extracellular metallo (Zn) DD-peptidase of Streptomyces albus G."; RL FEMS Microbiol. Lett. 59:215-219(1990). RN [2] RP PROTEIN SEQUENCE OF 43-255. RC STRAIN=Solvifaciens; RX PubMed=6825689; DOI=10.1111/j.1432-1033.1983.tb07116.x; RA Joris B., van Beeumen J., Casagrande F., Gerday C., Frere J.-M., RA Ghuysen J.-M.; RT "The complete amino acid sequence of the Zn2+-containing D-alanyl-D- RT alanine-cleaving carboxypeptidase of streptomyces albus G."; RL Eur. J. Biochem. 130:53-69(1983). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=7121588; DOI=10.1038/299469a0; RA Dideberg O., Charlier P., Dive G., Joris B., Frere J.-M., Ghuysen J.-M.; RT "Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving RT carboxypeptidase at 2.5-A resolution."; RL Nature 299:469-470(1982). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RA Wery J.-P., Charlier P., Dideberg O.; RL Submitted (MAR-1996) to the PDB data bank. CC -!- FUNCTION: This enzyme catalyzes carboxypeptidation and transpeptidation CC reactions involved in bacterial cell wall metabolism. It effectively CC catalyzes the transfer of the N-alpha, N-epsilon-diacetyl-L-lysyl-D- CC alanyl electrophilic group of the standard tripeptide substrate N- CC alpha,N-epsilon-diacetyl-L-lysyl-D-alanyl-D-alanine to water. It also CC performs a weak beta-lactamase activity, hydrolyzing penicillin into CC penicilloate at a very low rate. CC -!- CATALYTIC ACTIVITY: CC Reaction=Cleavage of the bond: (Ac)2-L-lysyl-D-alanyl-|-D-alanine.; CC EC=3.4.17.14; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- PTM: The N-terminus is partially blocked as a result of the cyclization CC of the first two amino acids into anhydroaspartylglycine imide. CC -!- SIMILARITY: Belongs to the peptidase M15 family. {ECO:0000305}. 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; X55794; CAA39319.1; -; Genomic_DNA. DR PIR; A60997; CPSMMU. DR PDB; 1LBU; X-ray; 1.80 A; A=43-255. DR AlphaFoldDB; P00733; -. DR MDposit; P00733; -. DR SMR; P00733; -. DR MEROPS; M15.001; -. DR EvolutionaryTrace; P00733; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0009046; F:zinc D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC. DR CDD; cd14844; Zn-DD-carboxypeptidase_like; 1. DR Gene3D; 3.30.1380.10; -; 1. DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1. DR InterPro; IPR013230; Peptidase_M15A_C. DR InterPro; IPR002477; Peptidoglycan-bd-like. DR InterPro; IPR036365; PGBD-like_sf. DR InterPro; IPR036366; PGBDSf. DR InterPro; IPR009045; Zn_M74/Hedgehog-like. DR Pfam; PF08291; Peptidase_M15_3; 1. DR Pfam; PF01471; PG_binding_1; 1. DR SUPFAM; SSF55166; Hedgehog/DD-peptidase; 1. DR SUPFAM; SSF47090; PGBD-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Carboxypeptidase; Cell wall biogenesis/degradation; KW Direct protein sequencing; Disulfide bond; Hydrolase; Metal-binding; KW Metalloprotease; Protease; Secreted; Signal; Zinc. FT SIGNAL 1..42 FT /evidence="ECO:0000269|PubMed:6825689" FT CHAIN 43..255 FT /note="Zinc D-Ala-D-Ala carboxypeptidase" FT /id="PRO_0000026754" FT ACT_SITE 234 FT /note="Proton donor" FT /evidence="ECO:0000255" FT BINDING 180 FT /ligand="substrate" FT /evidence="ECO:0000255" FT BINDING 196 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:6825689" FT BINDING 237 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:6825689" FT BINDING 239 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:6825689" FT MOD_RES 43 FT /note="Blocked amino end (Asp)" FT DISULFID 45..123 FT /evidence="ECO:0000269|PubMed:6825689" FT DISULFID 136..184 FT /evidence="ECO:0000269|PubMed:6825689" FT DISULFID 212..253 FT /evidence="ECO:0000269|PubMed:6825689" FT CONFLICT 43 FT /note="D -> N (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 110 FT /note="Missing (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:1LBU" FT HELIX 59..67 FT /evidence="ECO:0007829|PDB:1LBU" FT TURN 68..70 FT /evidence="ECO:0007829|PDB:1LBU" FT STRAND 81..83 FT /evidence="ECO:0007829|PDB:1LBU" FT HELIX 86..98 FT /evidence="ECO:0007829|PDB:1LBU" FT HELIX 109..118 FT /evidence="ECO:0007829|PDB:1LBU" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:1LBU" FT TURN 130..133 FT /evidence="ECO:0007829|PDB:1LBU" FT STRAND 142..145 FT /evidence="ECO:0007829|PDB:1LBU" FT HELIX 147..167 FT /evidence="ECO:0007829|PDB:1LBU" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:1LBU" FT HELIX 182..188 FT /evidence="ECO:0007829|PDB:1LBU" FT HELIX 195..198 FT /evidence="ECO:0007829|PDB:1LBU" FT STRAND 201..204 FT /evidence="ECO:0007829|PDB:1LBU" FT TURN 207..209 FT /evidence="ECO:0007829|PDB:1LBU" FT HELIX 211..217 FT /evidence="ECO:0007829|PDB:1LBU" FT HELIX 218..220 FT /evidence="ECO:0007829|PDB:1LBU" FT STRAND 224..227 FT /evidence="ECO:0007829|PDB:1LBU" FT STRAND 235..241 FT /evidence="ECO:0007829|PDB:1LBU" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:1LBU" FT STRAND 247..249 FT /evidence="ECO:0007829|PDB:1LBU" FT HELIX 251..253 FT /evidence="ECO:0007829|PDB:1LBU" SQ SEQUENCE 255 AA; 26190 MW; 9168C2145A863AD3 CRC64; MRPRPIRLLL TALVGAGLAF APVSAVAAPT ATASASADVG ALDGCYTWSG TLSEGSSGEA VRQLQIRVAG YPGTGAQLAI DGQFGPATKA AVQRFQSAYG LAADGIAGPA TFNKIYQLQD DDCTPVNFTY AELNRCNSDW SGGKVSAATA RANALVTMWK LQAMRHAMGD KPITVNGGFR SVTCNSNVGG ASNSRHMYGH AADLGAGSQG FCALAQAARN HGFTEILGPG YPGHNDHTHV AGGDGRFWSA PSCGI //