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Protein

D-alanyl-D-alanine carboxypeptidase

Gene
N/A
Organism
Streptomyces sp. (strain R61)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes distinct carboxypeptidation and transpeptidation reactions during the last stages of wall peptidoglycan synthesis. Mistaking a beta-lactam antibiotic molecule for a normal substrate (i.e. a D-alanyl-D-alanine-terminated peptide), it becomes immobilized in the form of a long-lived, serine-ester-linked acyl enzyme and thus behave as penicillin-binding protein (PBP).

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 sitei93Acyl-ester intermediate1
Binding sitei316Substrate1

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

MEROPSiS12.001.

Names & Taxonomyi

Protein namesi
Recommended name:
D-alanyl-D-alanine carboxypeptidase (EC:3.4.16.4)
Short name:
DD-carboxypeptidase
Short name:
DD-peptidase
OrganismiStreptomyces sp. (strain R61)
Taxonomic identifieri31952 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3350.
DrugBankiDB00456. Cefalotin.
DB03843. Formaldehyde.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Add BLAST31
ChainiPRO_000001705032 – 380D-alanyl-D-alanine carboxypeptidaseAdd BLAST349
PropeptideiPRO_0000017051381 – 406Add BLAST26

Structurei

Secondary structure

1406
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi39 – 51Combined sources13
Beta strandi55 – 63Combined sources9
Beta strandi66 – 75Combined sources10
Turni77 – 79Combined sources3
Beta strandi88 – 90Combined sources3
Helixi92 – 94Combined sources3
Helixi95 – 108Combined sources14
Helixi118 – 121Combined sources4
Beta strandi125 – 127Combined sources3
Helixi133 – 137Combined sources5
Helixi147 – 150Combined sources4
Beta strandi151 – 153Combined sources3
Helixi154 – 161Combined sources8
Helixi168 – 176Combined sources9
Beta strandi181 – 183Combined sources3
Helixi192 – 206Combined sources15
Helixi210 – 217Combined sources8
Turni218 – 223Combined sources6
Beta strandi238 – 240Combined sources3
Turni263 – 265Combined sources3
Helixi266 – 268Combined sources3
Helixi275 – 286Combined sources12
Helixi293 – 299Combined sources7
Beta strandi303 – 306Combined sources4
Beta strandi309 – 311Combined sources3
Beta strandi316 – 319Combined sources4
Beta strandi325 – 333Combined sources9
Beta strandi336 – 342Combined sources7
Beta strandi346 – 358Combined sources13
Helixi360 – 374Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CEFX-ray2.04A32-380[»]
1CEGX-ray1.80A32-380[»]
1HVBX-ray1.17A32-380[»]
1IKGX-ray1.90A32-380[»]
1IKIX-ray1.25A32-380[»]
1MPLX-ray1.12A32-380[»]
1PW1X-ray1.20A32-380[»]
1PW8X-ray1.30A32-380[»]
1PWCX-ray1.10A32-380[»]
1PWDX-ray1.20A32-380[»]
1PWGX-ray1.07A32-380[»]
1SCWX-ray1.13A32-380[»]
1SDEX-ray1.15A32-378[»]
1YQSX-ray1.05A32-380[»]
2PTEmodel-E32-380[»]
3PTEX-ray1.60A32-380[»]
ProteinModelPortaliP15555.
SMRiP15555.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15555.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni151 – 154Substrate binding4
Regioni190 – 192Substrate binding3
Regioni330 – 332Substrate binding3
Regioni357 – 358Substrate binding2

Sequence similaritiesi

Belongs to the peptidase S12 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
[Graphical view]
PfamiPF00144. Beta-lactamase. 1 hit.
[Graphical view]
SUPFAMiSSF56601. SSF56601. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P15555-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSGTVGRGT ALGAVLLALL AVPAQAGTAA AADLPAPDDT GLQAVLHTAL
60 70 80 90 100
SQGAPGAMVR VDDNGTIHQL SEGVADRATG RAITTTDRFR VGSVTKSFSA
110 120 130 140 150
VVLLQLVDEG KLDLDASVNT YLPGLLPDDR ITVRQVMSHR SGLYDYTNDM
160 170 180 190 200
FAQTVPGFES VRNKVFSYQD LITLSLKHGV TNAPGAAYSY SNTNFVVAGM
210 220 230 240 250
LIEKLTGHSV ATEYQNRIFT PLNLTDTFYV HPDTVIPGTH ANGYLTPDEA
260 270 280 290 300
GGALVDSTEQ TVSWAQSAGA VISSTQDLDT FFSALMSGQL MSAAQLAQMQ
310 320 330 340 350
QWTTVNSTQG YGLGLRRRDL SCGISVYGHT GTVQGYYTYA FASKDGKRSV
360 370 380 390 400
TALANTSNNV NVLNTMARTL ESAFCGKPTT AKLRSATSSA TTVERHEDIA

PGIARD
Length:406
Mass (Da):42,917
Last modified:February 1, 1996 - v2
Checksum:iC2C77B53A29099E9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05109 Genomic DNA. Translation: CAA28756.1.
X55810 Genomic DNA. Translation: CAB97254.1.
PIRiS48220.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05109 Genomic DNA. Translation: CAA28756.1.
X55810 Genomic DNA. Translation: CAB97254.1.
PIRiS48220.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CEFX-ray2.04A32-380[»]
1CEGX-ray1.80A32-380[»]
1HVBX-ray1.17A32-380[»]
1IKGX-ray1.90A32-380[»]
1IKIX-ray1.25A32-380[»]
1MPLX-ray1.12A32-380[»]
1PW1X-ray1.20A32-380[»]
1PW8X-ray1.30A32-380[»]
1PWCX-ray1.10A32-380[»]
1PWDX-ray1.20A32-380[»]
1PWGX-ray1.07A32-380[»]
1SCWX-ray1.13A32-380[»]
1SDEX-ray1.15A32-378[»]
1YQSX-ray1.05A32-380[»]
2PTEmodel-E32-380[»]
3PTEX-ray1.60A32-380[»]
ProteinModelPortaliP15555.
SMRiP15555.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

ChEMBLiCHEMBL3350.
DrugBankiDB00456. Cefalotin.
DB03843. Formaldehyde.

Protein family/group databases

MEROPSiS12.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00219.
BRENDAi3.4.16.4. 1284.

Miscellaneous databases

EvolutionaryTraceiP15555.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
[Graphical view]
PfamiPF00144. Beta-lactamase. 1 hit.
[Graphical view]
SUPFAMiSSF56601. SSF56601. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDAC_STRSR
AccessioniPrimary (citable) accession number: P15555
Secondary accession number(s): Q06656
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 1996
Last modified: November 2, 2016
This is version 108 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. 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.