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P00733 (CBPM_STRAL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismStreptomyces albus G
Taxonomic identifier1962 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processCell wall biogenesis/degradation
   Cellular componentSecreted
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionCarboxypeptidase
Hydrolase
Metalloprotease
Protease
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc D-Ala-D-Ala carboxypeptidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4242 Ref.2
Chain43 – 255213Zinc D-Ala-D-Ala carboxypeptidase
PRO_0000026754

Sites

Active site2341Proton donor Potential
Metal binding1961Zinc; catalytic Ref.2
Metal binding2371Zinc; catalytic Ref.2
Metal binding2391Zinc; catalytic Ref.2
Binding site1801Substrate Potential

Amino acid modifications

Modified residue431Blocked amino end (Asp)
Disulfide bond45 ↔ 123 Ref.2
Disulfide bond136 ↔ 184 Ref.2
Disulfide bond212 ↔ 253 Ref.2

Experimental info

Sequence conflict431D → N AA sequence Ref.2
Sequence conflict1101Missing AA sequence Ref.2

Secondary structure

......................................... 255
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00733 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 9168C2145A863AD3

FASTA25526,190
        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 

« Hide

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.
PIRCPSMMU. A60997.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LBUX-ray1.80A43-255[»]
ProteinModelPortalP00733.
SMRP00733. Positions 43-255.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM15.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.101.10. 1 hit.
3.30.1380.10. 1 hit.
InterProIPR009045. Hedgehog_sig/DD-Pept_Zn-bd_dom.
IPR013230. Peptidase_M15A_C.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamPF08291. Peptidase_M15_3. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF55166. SSF55166. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP00733.

Entry information

Entry nameCBPM_STRAL
AccessionPrimary (citable) accession number: P00733
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1995
Last modified: May 14, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references