CBPM_STRAL
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 03-AUG-2022, entry version 128.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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}.
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DR EMBL; X55794; CAA39319.1; -; Genomic_DNA.
DR PIR; A60997; CPSMMU.
DR PDB; 1LBU; X-ray; 1.80 A; A=43-255.
DR PDBsum; 1LBU; -.
DR AlphaFoldDB; P00733; -.
DR SMR; P00733; -.
DR MEROPS; M15.001; -.
DR EvolutionaryTrace; P00733; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009046; F:zinc D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.101.10; -; 1.
DR Gene3D; 3.30.1380.10; -; 1.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR013230; Peptidase_M15A_C.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR Pfam; PF08291; Peptidase_M15_3; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR SUPFAM; SSF55166; SSF55166; 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 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
