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P00733

- CBPM_STRAL

UniProt

P00733 - CBPM_STRAL

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
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    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 – 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

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

    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

    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.
    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

    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

    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:
    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: October 1, 2014
    This is version 105 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