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P00733

- CBPM_STRAL

UniProt

P00733 - CBPM_STRAL

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Protein

Zinc D-Ala-D-Ala carboxypeptidase

Gene
N/A
Organism
Streptomyces albus G
Status
Reviewed - 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

Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei180 – 1801Substrate Reviewed prediction
Metal bindingi196 – 1961Zinc; catalytic1 Publication
Active sitei234 – 2341Proton donor Reviewed prediction
Metal bindingi237 – 2371Zinc; catalytic1 Publication
Metal bindingi239 – 2391Zinc; catalytic1 Publication

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. zinc D-Ala-D-Ala carboxypeptidase activity Source: UniProtKB-EC
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

  1. extracellular region Source: UniProtKB-SubCell
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 – 679
Turni68 – 703
Beta strandi81 – 833
Helixi86 – 9813
Helixi109 – 11810
Beta strandi123 – 1253
Turni130 – 1334
Beta strandi142 – 1454
Helixi147 – 16721
Beta strandi175 – 1773
Helixi182 – 1887
Helixi195 – 1984
Beta strandi201 – 2044
Turni207 – 2093
Helixi211 – 2177
Helixi218 – 2203
Beta strandi224 – 2274
Beta strandi235 – 2417
Beta strandi243 – 2453
Beta strandi247 – 2493
Helixi251 – 2533

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LBUX-ray1.80A43-255[»]
ProteinModelPortaliP00733.
SMRiP00733. Positions 43-255.

Miscellaneous databases

EvolutionaryTraceiP00733.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M15 family.

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

MRPRPIRLLL TALVGAGLAF APVSAVAAPT ATASASADVG ALDGCYTWSG    50
TLSEGSSGEA VRQLQIRVAG YPGTGAQLAI DGQFGPATKA AVQRFQSAYG 100
LAADGIAGPA TFNKIYQLQD DDCTPVNFTY AELNRCNSDW SGGKVSAATA 150
RANALVTMWK LQAMRHAMGD KPITVNGGFR SVTCNSNVGG ASNSRHMYGH 200
AADLGAGSQG FCALAQAARN HGFTEILGPG YPGHNDHTHV AGGDGRFWSA 250
PSCGI 255
Length:255
Mass (Da):26,190
Last modified:February 1, 1995 - v2
Checksum:i9168C2145A863AD3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431D → N AA sequence 1 Publication
Sequence conflicti110 – 1101Missing AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55794 Genomic DNA. Translation: CAA39319.1.
PIRiA60997. CPSMMU.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55794 Genomic DNA. Translation: CAA39319.1 .
PIRi A60997. CPSMMU.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LBU X-ray 1.80 A 43-255 [» ]
ProteinModelPortali P00733.
SMRi P00733. Positions 43-255.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M15.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P00733.

Family and domain databases

Gene3Di 1.10.101.10. 1 hit.
3.30.1380.10. 1 hit.
InterProi IPR009045. Hedgehog_sig/DD-Pept_Zn-bd_dom.
IPR013230. Peptidase_M15A_C.
IPR002477. Peptidoglycan-bd-like.
[Graphical view ]
Pfami PF08291. Peptidase_M15_3. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
SSF55166. SSF55166. 1 hit.
ProtoNeti Search...

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 14, 2014
This is version 104 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

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