P00733 (CBPM_STRAL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Zinc D-Ala-D-Ala carboxypeptidase EC=3.4.17.14 Alternative name(s): D-alanyl-D-alanine carboxypeptidase Metallo DD-peptidase Zn DD-peptidase
Organism	Streptomyces albus G
Taxonomic identifier	1962 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › Streptomyces albus

Protein attributes

Sequence length	255 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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	Binds 1 zinc ion per subunit.
Subcellular location	Secreted.
Post-translational modification	The N-terminus is partially blocked as a result of the cyclization of the first two amino acids into anhydroaspartylglycine imide.
Sequence similarities	Belongs to the peptidase M15 family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Carboxypeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW zinc D-Ala-D-Ala carboxypeptidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 42

42

Ref.2

Chain

43 – 255

213

Zinc D-Ala-D-Ala carboxypeptidase

PRO_0000026754

Sites

Active site

234

1

Proton donor Potential

Metal binding

196

1

Zinc; catalytic Ref.2

Metal binding

237

1

Zinc; catalytic Ref.2

Metal binding

239

1

Zinc; catalytic Ref.2

Binding site

180

1

Substrate Potential

Amino acid modifications

Modified residue

43

1

Blocked amino end (Asp)

Disulfide bond

45 ↔ 123

Ref.2

Disulfide bond

136 ↔ 184

Ref.2

Disulfide bond

212 ↔ 253

Ref.2

Experimental info

Sequence conflict

43

1

D → N AA sequence Ref.2

Sequence conflict

110

1

Missing AA sequence Ref.2

Secondary structure

1

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255

Helix Strand Turn

Details...

Helix

59 – 67

9

Turn

68 – 70

3

Beta strand

81 – 83

3

Helix

86 – 98

13

Helix

109 – 118

10

Beta strand

123 – 125

3

Turn

130 – 133

4

Beta strand

142 – 145

4

Helix

147 – 167

21

Beta strand

175 – 177

3

Helix

182 – 188

7

Helix

195 – 198

4

Beta strand

201 – 204

4

Turn

207 – 209

3

Helix

211 – 217

7

Helix

218 – 220

3

Beta strand

224 – 227

4

Beta strand

235 – 241

7

Beta strand

243 – 245

3

Beta strand

247 – 249

3

Helix

251 – 253

3

Sequences

	Sequence		Length	Mass (Da)
	P00733 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: 9168C2145A863AD3	FASTA	255	26,190
	10 20 30 40 50 60 MRPRPIRLLL TALVGAGLAF APVSAVAAPT ATASASADVG ALDGCYTWSG TLSEGSSGEA 70 80 90 100 110 120 VRQLQIRVAG YPGTGAQLAI DGQFGPATKA AVQRFQSAYG LAADGIAGPA TFNKIYQLQD 130 140 150 160 170 180 DDCTPVNFTY AELNRCNSDW SGGKVSAATA RANALVTMWK LQAMRHAMGD KPITVNGGFR 190 200 210 220 230 240 SVTCNSNVGG ASNSRHMYGH AADLGAGSQG FCALAQAARN HGFTEILGPG YPGHNDHTHV 250 AGGDGRFWSA PSCGI

References

[1]	"Cloning, nucleotide sequence and amplified expression of the gene encoding the extracellular metallo (Zn) DD-peptidase of Streptomyces albus G." Duez C., Lakaye B., Houba S., Dusart J., Ghuysen J.-M. FEMS Microbiol. Lett. 59:215-219(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: G.
[2]	"The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of streptomyces albus G." Joris B., van Beeumen J., Casagrande F., Gerday C., Frere J.-M., Ghuysen J.-M. Eur. J. Biochem. 130:53-69(1983) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 43-255. Strain: Solvifaciens.
[3]	"Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5-A resolution." Dideberg O., Charlier P., Dive G., Joris B., Frere J.-M., Ghuysen J.-M. Nature 299:469-470(1982) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[4]	Wery J.-P., Charlier P., Dideberg O. Submitted (MAR-1996) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X55794 Genomic DNA. Translation: CAA39319.1.

PIR

CPSMMU. A60997.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LBU	X-ray	1.80	A	43-255	[»]

ProteinModelPortal

P00733.

SMR

P00733. Positions 43-255.

ModBase

Search...

Protein family/group databases

MEROPS

M15.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.101.10. 1 hit.
3.30.1380.10. 1 hit.

InterPro

IPR009045. Hedgehog_sig/DD-Pept_Zn-bd_dom.
IPR013230. Peptidase_M15A_C.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]

Pfam

PF08291. Peptidase_M15_3. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]

SUPFAM

SSF55166. Hedgehog_sig_N. 1 hit.
SSF47090. PGBD_like. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P00733.

Entry information

Entry name

CBPM_STRAL

Accession

Primary (citable) accession number: P00733

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	February 1, 1995
Last modified:	April 3, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program