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Protein

Zinc D-Ala-D-Ala carboxypeptidase

Gene
N/A
Organism
Streptomyces albus G
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Cleavage of the bond: (Ac)(2)-L-lysyl-D-alanyl-|-D-alanine.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei180 – 1801SubstrateSequence Analysis
Metal bindingi196 – 1961Zinc; catalytic1 Publication
Active sitei234 – 2341Proton donorSequence Analysis
Metal bindingi237 – 2371Zinc; catalytic1 Publication
Metal bindingi239 – 2391Zinc; catalytic1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cell wall biogenesis/degradation

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM15.001.

Names & Taxonomyi

Protein namesi
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
OrganismiStreptomyces albus G
Taxonomic identifieri1962 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 42421 PublicationAdd
BLAST
Chaini43 – 255213Zinc D-Ala-D-Ala carboxypeptidasePRO_0000026754Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431Blocked amino end (Asp)
Disulfide bondi45 ↔ 1231 Publication
Disulfide bondi136 ↔ 1841 Publication
Disulfide bondi212 ↔ 2531 Publication

Post-translational modificationi

The N-terminus is partially blocked as a result of the cyclization of the first two amino acids into anhydroaspartylglycine imide.

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
255
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi59 – 679Combined sources
Turni68 – 703Combined sources
Beta strandi81 – 833Combined sources
Helixi86 – 9813Combined sources
Helixi109 – 11810Combined sources
Beta strandi123 – 1253Combined sources
Turni130 – 1334Combined sources
Beta strandi142 – 1454Combined sources
Helixi147 – 16721Combined sources
Beta strandi175 – 1773Combined sources
Helixi182 – 1887Combined sources
Helixi195 – 1984Combined sources
Beta strandi201 – 2044Combined sources
Turni207 – 2093Combined sources
Helixi211 – 2177Combined sources
Helixi218 – 2203Combined sources
Beta strandi224 – 2274Combined sources
Beta strandi235 – 2417Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi247 – 2493Combined sources
Helixi251 – 2533Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LBUX-ray1.80A43-255[»]
ProteinModelPortaliP00733.
SMRiP00733. Positions 43-255.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00733.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M15 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
3.30.1380.10. 1 hit.
InterProiIPR009045. Hedgehog_sig/DD-Pept_Zn-bd_dom.
IPR013230. Peptidase_M15A_C.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF08291. Peptidase_M15_3. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF55166. SSF55166. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00733-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPRPIRLLL TALVGAGLAF APVSAVAAPT ATASASADVG ALDGCYTWSG
60 70 80 90 100
TLSEGSSGEA VRQLQIRVAG YPGTGAQLAI DGQFGPATKA AVQRFQSAYG
110 120 130 140 150
LAADGIAGPA TFNKIYQLQD DDCTPVNFTY AELNRCNSDW SGGKVSAATA
160 170 180 190 200
RANALVTMWK LQAMRHAMGD KPITVNGGFR SVTCNSNVGG ASNSRHMYGH
210 220 230 240 250
AADLGAGSQG FCALAQAARN HGFTEILGPG YPGHNDHTHV AGGDGRFWSA

PSCGI
Length:255
Mass (Da):26,190
Last modified:February 1, 1995 - v2
Checksum:i9168C2145A863AD3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431D → N AA sequence (PubMed:6825689).Curated
Sequence conflicti110 – 1101Missing AA sequence (PubMed:6825689).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55794 Genomic DNA. Translation: CAA39319.1.
PIRiA60997. CPSMMU.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55794 Genomic DNA. Translation: CAA39319.1.
PIRiA60997. CPSMMU.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LBUX-ray1.80A43-255[»]
ProteinModelPortaliP00733.
SMRiP00733. Positions 43-255.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM15.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00733.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
3.30.1380.10. 1 hit.
InterProiIPR009045. Hedgehog_sig/DD-Pept_Zn-bd_dom.
IPR013230. Peptidase_M15A_C.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF08291. Peptidase_M15_3. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF55166. SSF55166. 1 hit.
ProtoNetiSearch...

Publicationsi

  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).

Entry informationi

Entry nameiCBPM_STRAL
AccessioniPrimary (citable) accession number: P00733
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1995
Last modified: May 27, 2015
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.