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Protein

D-alanyl-D-alanine carboxypeptidase

Gene
N/A
Organism
Streptomyces sp. (strain K15)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.

Catalytic activityi

Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.

Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei64Acyl-ester intermediate1 Publication1
Active sitei67Proton acceptor1 Publication1
Active sitei1251 Publication1
Binding sitei242Substrate1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BRENDAi3.4.16.4. 1284.
UniPathwayiUPA00219.

Protein family/group databases

MEROPSiS11.004.

Names & Taxonomyi

Protein namesi
Recommended name:
D-alanyl-D-alanine carboxypeptidase (EC:3.4.16.4)
Short name:
DD-carboxypeptidase
Short name:
DD-peptidase
Alternative name(s):
Penicillin-binding protein
Short name:
PBP
OrganismiStreptomyces sp. (strain K15)
Taxonomic identifieri1958 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi67K → H: Almost no activity. 1 Publication1
Mutagenesisi125S → A: Almost no activity. 1 Publication1
Mutagenesisi127C → A or N: 10% of wild-type catalytic efficiency for aminolysis reaction, but increased catalytic efficiency for hydrolysis reaction. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 291 PublicationAdd BLAST29
ChainiPRO_000002723630 – 291D-alanyl-D-alanine carboxypeptidaseAdd BLAST262

Structurei

Secondary structure

1291
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 44Combined sources7
Turni45 – 47Combined sources3
Beta strandi50 – 55Combined sources6
Helixi63 – 66Combined sources4
Helixi67 – 75Combined sources9
Beta strandi85 – 87Combined sources3
Helixi90 – 98Combined sources9
Beta strandi111 – 113Combined sources3
Helixi114 – 122Combined sources9
Helixi127 – 137Combined sources11
Beta strandi140 – 142Combined sources3
Helixi143 – 160Combined sources18
Beta strandi169 – 172Combined sources4
Helixi183 – 193Combined sources11
Helixi197 – 203Combined sources7
Beta strandi206 – 208Combined sources3
Beta strandi211 – 213Combined sources3
Beta strandi219 – 221Combined sources3
Helixi231 – 234Combined sources4
Beta strandi238 – 246Combined sources9
Turni247 – 249Combined sources3
Beta strandi250 – 259Combined sources10
Beta strandi262 – 273Combined sources12
Helixi274 – 290Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ES2X-ray1.55A30-291[»]
1ES3X-ray2.20A30-291[»]
1ES4X-ray1.90A30-291[»]
1ES5X-ray1.40A30-291[»]
1ESIX-ray1.80A30-291[»]
1J9MX-ray1.65A30-291[»]
1SKFX-ray2.00A30-291[»]
ProteinModelPortaliP39042.
SMRiP39042.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39042.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S11 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR018044. Peptidase_S11.
IPR001967. Peptidase_S11_N.
[Graphical view]
PfamiPF00768. Peptidase_S11. 1 hit.
[Graphical view]
PRINTSiPR00725. DADACBPTASE1.
SUPFAMiSSF56601. SSF56601. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P39042-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLRRAAATV ITTGALLAAG TLGATPATAV TKPTIAAVGG YAMNNGTGTT
60 70 80 90 100
LYTKAADTRR STGSTTKIMT AKVVLAQSNL NLDAKVTIQK AYSDYVVANK
110 120 130 140 150
PSQAHLIVGD KVTVRQLLYG LMLPSGCDAA YALADKYGSG SQAAARVKSF
160 170 180 190 200
IGKMNTAATN LGLHNTHFDS FDGIGNGANY STPRHLTKIA SSAMKNSTFR
210 220 230 240 250
TVVKTKAYTA KTVTKTGSIR TMDTWKNTNG LLSSYSGAIG VKTGSGPEAK
260 270 280 290
YCLVFAATRG GKTVIGTVLA STSIPARESD ATKIMNYGFA L
Length:291
Mass (Da):30,258
Last modified:February 1, 1995 - v1
Checksum:iF31039CC7DB0962B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti70T → Q AA sequence (PubMed:2764892).Curated1
Sequence conflicti83D → S AA sequence (PubMed:2764892).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59965 Genomic DNA. Translation: CAA42591.1.
PIRiS17674.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59965 Genomic DNA. Translation: CAA42591.1.
PIRiS17674.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ES2X-ray1.55A30-291[»]
1ES3X-ray2.20A30-291[»]
1ES4X-ray1.90A30-291[»]
1ES5X-ray1.40A30-291[»]
1ESIX-ray1.80A30-291[»]
1J9MX-ray1.65A30-291[»]
1SKFX-ray2.00A30-291[»]
ProteinModelPortaliP39042.
SMRiP39042.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS11.004.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00219.
BRENDAi3.4.16.4. 1284.

Miscellaneous databases

EvolutionaryTraceiP39042.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR018044. Peptidase_S11.
IPR001967. Peptidase_S11_N.
[Graphical view]
PfamiPF00768. Peptidase_S11. 1 hit.
[Graphical view]
PRINTSiPR00725. DADACBPTASE1.
SUPFAMiSSF56601. SSF56601. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDACX_STRSK
AccessioniPrimary (citable) accession number: P39042
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 90 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.