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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)DescriptionActionsGraphical viewLength
Binding sitei180SubstrateSequence analysis1
Metal bindingi196Zinc; catalytic1 Publication1
Active sitei234Proton donorSequence analysis1
Metal bindingi237Zinc; catalytic1 Publication1
Metal bindingi239Zinc; catalytic1 Publication1

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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 421 PublicationAdd BLAST42
ChainiPRO_000002675443 – 255Zinc D-Ala-D-Ala carboxypeptidaseAdd BLAST213

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43Blocked amino end (Asp)1
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

1255
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi59 – 67Combined sources9
Turni68 – 70Combined sources3
Beta strandi81 – 83Combined sources3
Helixi86 – 98Combined sources13
Helixi109 – 118Combined sources10
Beta strandi123 – 125Combined sources3
Turni130 – 133Combined sources4
Beta strandi142 – 145Combined sources4
Helixi147 – 167Combined sources21
Beta strandi175 – 177Combined sources3
Helixi182 – 188Combined sources7
Helixi195 – 198Combined sources4
Beta strandi201 – 204Combined sources4
Turni207 – 209Combined sources3
Helixi211 – 217Combined sources7
Helixi218 – 220Combined sources3
Beta strandi224 – 227Combined sources4
Beta strandi235 – 241Combined sources7
Beta strandi243 – 245Combined sources3
Beta strandi247 – 249Combined sources3
Helixi251 – 253Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LBUX-ray1.80A43-255[»]
ProteinModelPortaliP00733.
SMRiP00733.
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)DescriptionActionsGraphical viewLength
Sequence conflicti43D → N AA sequence (PubMed:6825689).Curated1
Sequence conflicti110Missing AA sequence (PubMed:6825689).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LBUX-ray1.80A43-255[»]
ProteinModelPortaliP00733.
SMRiP00733.
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...

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: November 2, 2016
This is version 116 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

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 one 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.