dacA:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

DacA

Synonyms

D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 5)[1], B0632[2][1], Pfv[2][1], DacA[2][1], PBP5, ECK0625, JW0627, pfv, b0632

Product description

D-alanyl-D-alanine carboxypeptidase, fraction A; penicillin-binding protein 5[2][3]

D-alanine D-alanine carboxypeptidase PBP5, cell morphology; penicillin-binding protein 5; beta-lactamase activity[4]

EC number (for enzymes)
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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0030288

outer membrane-bounded periplasmic space

C

Seeded from Riley et al 2006 [1].

Missing: evidence, reference

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

PMID:368033[5]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

PMID:1740130[6]

IDA: Inferred from Direct Assay

F

complete

GO:0006508

proteolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001967

P

Seeded from EcoCyc (v14.0)

complete

GO:0005887

integral to plasma membrane

PMID:319999[7]

IDA: Inferred from Direct Assay

C

complete

GO:0006508

proteolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012907

P

Seeded from EcoCyc (v14.0)

complete

GO:0006508

proteolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015956

P

Seeded from EcoCyc (v14.0)

complete

GO:0006508

proteolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR018044

P

Seeded from EcoCyc (v14.0)

complete

GO:0008360

regulation of cell shape

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0133

P

Seeded from EcoCyc (v14.0)

complete

GO:0008800

beta-lactamase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:3.5.2.6

F

Seeded from EcoCyc (v14.0)

complete

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001967

F

Seeded from EcoCyc (v14.0)

complete

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012907

F

Seeded from EcoCyc (v14.0)

complete

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR018044

F

Seeded from EcoCyc (v14.0)

complete

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:3.4.16.4

F

Seeded from EcoCyc (v14.0)

complete

GO:0009252

peptidoglycan biosynthetic process

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0573

P

Seeded from EcoCyc (v14.0)

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

glpD

PMID:19402753[8]

LCMS(ID Probability):99.6

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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

Inner membrane

PMID:3279397[9], PMID:8424800[10], PMID:8486152[11]

EchoLocation:dacA

Membrane anchored

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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MNTIFSARIM KRLALTTALC TAFISAAHAD DLNIKTMIPG VPQIDAESYI LIDYNSGKVL
AEQNADVRRD PASLTKMMTS YVIGQAMKAG KFKETDLVTI GNDAWATGNP VFKGSSLMFL
KPGMQVPVSQ LIRGINLQSG NDACVAMADF AAGSQDAFVG LMNSYVNALG LKNTHFQTVH
GLDADGQYSS ARDMALIGQA LIRDVPNEYS IYKEKEFTFN GIRQLNRNGL LWDNSLNVDG
IKTGHTDKAG YNLVASATEG QMRLISAVMG GRTFKGREAE SKKLLTWGFR FFETVNPLKV
GKEFASEPVW FGDSDRASLG VDKDVYLTIP RGRMKDLKAS YVLNSSELHA PLQKNQVVGT
INFQLDGKTI EQRPLVVLQE IPEGNFFGKI IDYIKLMFHH WFG
Length

403

Mol. Wt

44.445 kDa

pI

8.5 (calculated)

Extinction coefficient

43,890 - 44,140 (calc based on 11 Y, 5 W, and 2 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

motif

1-29

UniProt Manual:Signal Peptides

UniProt:P0AEB2

Modification Site

345

phosphorylation site at S345

probability greater than 75%

PMID:17938405[12]

Domain

35..273

PF00768 D-alanyl-D-alanine carboxypeptidase

PMID:19920124[13]

Domain

292..383

PF07943 Penicillin-binding protein 5, C-terminal domain

PMID:19920124[13]

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Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=dacA taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16128615

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:945222

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0002168

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0AEB2

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10201

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10201

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:945222

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000195

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0197

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ Matsuhashi, M et al. (1979) Mutational evidence for identity of penicillin-binding protein 5 in Escherichia coli with the major D-alanine carboxypeptidase IA activity. J. Bacteriol. 137 644-7 PubMed
  6. ↑ van der Linden, MP et al. (1992) Cytoplasmic high-level expression of a soluble, enzymatically active form of the Escherichia coli penicillin-binding protein 5 and purification by dye chromatography. Eur. J. Biochem. 204 197-202 PubMed
  7. ↑ Spratt, BG (1977) Properties of the penicillin-binding proteins of Escherichia coli K12,. Eur. J. Biochem. 72 341-52 PubMed
  8. ↑ Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  9. ↑ Broome-Smith, JK et al. (1988) Nucleotide sequences of the penicillin-binding protein 5 and 6 genes of Escherichia coli. Nucleic Acids Res. 16 1617 PubMed
  10. ↑ van der Linden, MP et al. (1993) Domain organization of penicillin-binding protein 5 from Escherichia coli analysed by C-terminal truncation. Biochem. J. 289 ( Pt 2) 593-8 PubMed
  11. ↑ Phoenix, DA & Pratt, JM (1993) Membrane interaction of Escherichia coli penicillin binding protein 5 is modulated by the ectomembranous domain. FEBS Lett. 322 215-8 PubMed
  12. ↑ Macek, B et al. (2008) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol. Cell Proteomics 7 299-307 PubMed
  13. ↑ 13.0 13.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

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