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Zinc D-Ala-D-Ala carboxypeptidase (EC 3.4.17.14) (D-alanyl-D-alanine carboxypeptidase) (Metallo DD-peptidase) (Zn DD-peptidase)

 CBPM_STRAL              Reviewed;         255 AA.
P00733;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 2.
23-MAY-2018, entry version 119.
RecName: Full=Zinc D-Ala-D-Ala carboxypeptidase;
EC=3.4.17.14;
AltName: Full=D-alanyl-D-alanine carboxypeptidase;
AltName: Full=Metallo DD-peptidase;
AltName: Full=Zn DD-peptidase;
Flags: Precursor;
Streptomyces albus G.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1962;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=G;
PubMed=2276609; DOI=10.1016/0378-1097(90)90059-Y;
Duez C., Lakaye B., Houba S., Dusart J., Ghuysen J.-M.;
"Cloning, nucleotide sequence and amplified expression of the gene
encoding the extracellular metallo (Zn) DD-peptidase of Streptomyces
albus G.";
FEMS Microbiol. Lett. 59:215-219(1990).
[2]
PROTEIN SEQUENCE OF 43-255.
STRAIN=Solvifaciens;
PubMed=6825689;
Joris B., van Beeumen J., Casagrande F., Gerday C., Frere J.-M.,
Ghuysen J.-M.;
"The complete amino acid sequence of the Zn2+-containing D-alanyl-D-
alanine-cleaving carboxypeptidase of streptomyces albus G.";
Eur. J. Biochem. 130:53-69(1983).
[3]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=7121588; DOI=10.1038/299469a0;
Dideberg O., Charlier P., Dive G., Joris B., Frere J.-M.,
Ghuysen J.-M.;
"Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving
carboxypeptidase at 2.5-A resolution.";
Nature 299:469-470(1982).
[4]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Wery J.-P., Charlier P., Dideberg O.;
Submitted (MAR-1996) to the PDB data bank.
-!- FUNCTION: This enzyme catalyzes carboxypeptidation and
transpeptidation reactions involved in bacterial cell wall
metabolism. It effectively catalyzes the transfer of the N-alpha,
N-epsilon-diacetyl-L-lysyl-D-alanyl electrophilic group of the
standard tripeptide substrate N-alpha,N-epsilon-diacetyl-L-lysyl-
D-alanyl-D-alanine to water. It also performs a weak beta-
lactamase activity, hydrolyzing penicillin into penicilloate at a
very low rate.
-!- CATALYTIC ACTIVITY: Cleavage of the bond: (Ac)(2)-L-lysyl-D-
alanyl-|-D-alanine.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: The N-terminus is partially blocked as a result of the
cyclization of the first two amino acids into
anhydroaspartylglycine imide.
-!- SIMILARITY: Belongs to the peptidase M15 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X55794; CAA39319.1; -; Genomic_DNA.
PIR; A60997; CPSMMU.
PDB; 1LBU; X-ray; 1.80 A; A=43-255.
PDBsum; 1LBU; -.
ProteinModelPortal; P00733; -.
SMR; P00733; -.
MEROPS; M15.001; -.
PRIDE; P00733; -.
EvolutionaryTrace; P00733; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009046; F:zinc D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
Gene3D; 1.10.101.10; -; 1.
Gene3D; 3.30.1380.10; -; 1.
InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
InterPro; IPR013230; Peptidase_M15A_C.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
InterPro; IPR036366; PGBDSf.
Pfam; PF08291; Peptidase_M15_3; 1.
Pfam; PF01471; PG_binding_1; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF55166; SSF55166; 1.
1: Evidence at protein level;
3D-structure; Carboxypeptidase; Cell wall biogenesis/degradation;
Direct protein sequencing; Disulfide bond; Hydrolase; Metal-binding;
Metalloprotease; Protease; Secreted; Signal; Zinc.
SIGNAL 1 42 {ECO:0000269|PubMed:6825689}.
CHAIN 43 255 Zinc D-Ala-D-Ala carboxypeptidase.
/FTId=PRO_0000026754.
ACT_SITE 234 234 Proton donor. {ECO:0000255}.
METAL 196 196 Zinc; catalytic.
{ECO:0000269|PubMed:6825689}.
METAL 237 237 Zinc; catalytic.
{ECO:0000269|PubMed:6825689}.
METAL 239 239 Zinc; catalytic.
{ECO:0000269|PubMed:6825689}.
BINDING 180 180 Substrate. {ECO:0000255}.
MOD_RES 43 43 Blocked amino end (Asp).
DISULFID 45 123 {ECO:0000269|PubMed:6825689}.
DISULFID 136 184 {ECO:0000269|PubMed:6825689}.
DISULFID 212 253 {ECO:0000269|PubMed:6825689}.
CONFLICT 43 43 D -> N (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 110 110 Missing (in Ref. 2; AA sequence).
{ECO:0000305}.
HELIX 59 67 {ECO:0000244|PDB:1LBU}.
TURN 68 70 {ECO:0000244|PDB:1LBU}.
STRAND 81 83 {ECO:0000244|PDB:1LBU}.
HELIX 86 98 {ECO:0000244|PDB:1LBU}.
HELIX 109 118 {ECO:0000244|PDB:1LBU}.
STRAND 123 125 {ECO:0000244|PDB:1LBU}.
TURN 130 133 {ECO:0000244|PDB:1LBU}.
STRAND 142 145 {ECO:0000244|PDB:1LBU}.
HELIX 147 167 {ECO:0000244|PDB:1LBU}.
STRAND 175 177 {ECO:0000244|PDB:1LBU}.
HELIX 182 188 {ECO:0000244|PDB:1LBU}.
HELIX 195 198 {ECO:0000244|PDB:1LBU}.
STRAND 201 204 {ECO:0000244|PDB:1LBU}.
TURN 207 209 {ECO:0000244|PDB:1LBU}.
HELIX 211 217 {ECO:0000244|PDB:1LBU}.
HELIX 218 220 {ECO:0000244|PDB:1LBU}.
STRAND 224 227 {ECO:0000244|PDB:1LBU}.
STRAND 235 241 {ECO:0000244|PDB:1LBU}.
STRAND 243 245 {ECO:0000244|PDB:1LBU}.
STRAND 247 249 {ECO:0000244|PDB:1LBU}.
HELIX 251 253 {ECO:0000244|PDB:1LBU}.
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


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