dacC:Gene Product(s)
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Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
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 |
DacC |
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Synonyms |
D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 6a)[1], B0839[2][1], DacC[2][1], D-alanyl-D-alanine carboxypeptidase[2][1] , ECK0829, JW0823, b0839 |
Product description |
penicillin-binding protein 6[2][3] D-alanine D-alanine carboxypeptidase PBP6; penicillin-binding protein 6[4] |
EC number (for enzymes) | |
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Notes
Function
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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:0004180 |
carboxypeptidase activity |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005887 |
integral to plasma membrane |
IDA: Inferred from Direct Assay |
C |
complete | ||||
GO:0006508 |
proteolysis |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006508 |
proteolysis |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006508 |
proteolysis |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0006508 |
proteolysis |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0008360 |
regulation of cell shape |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0009002 |
serine-type D-Ala-D-Ala carboxypeptidase activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0009002 |
serine-type D-Ala-D-Ala carboxypeptidase activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0009002 |
serine-type D-Ala-D-Ala carboxypeptidase activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0009002 |
serine-type D-Ala-D-Ala carboxypeptidase activity |
GOA:spec |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0009252 |
peptidoglycan biosynthetic process |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0019898 |
extrinsic to membrane |
IEA: Inferred from Electronic Annotation |
SP_SL:SL-9903 |
C |
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 |
---|---|---|---|---|
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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 |
---|---|---|---|---|
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Notes
Structure and Physical Properties
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Physical Properties
See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.
Name | |
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Sequence |
MTQYSSLLRG LAAGSAFLFL FAPTAFAAEQ TVEAPSVDAR AWILMDYASG KVLAEGNADE KLDPASLTKI MTSYVVGQAL KADKIKLTDM VTVGKDAWAT GNPALRGSSV MFLKPGDQVS VADLNKGVII QSGNDACIAL ADYVAGSQES FIGLMNGYAK KLGLTNTTFQ TVHGLDAPGQ FSTARDMALL GKALIHDVPE EYAIHKEKEF TFNKIRQPNR NRLLWSSNLN VDGMKTGTTA GAGYNLVASA TQGDMRLISV VLGAKTDRIR FNESEKLLTW GFRFFETVTP IKPDATFVTQ RVWFGDKSEV NLGAGEAGSV TIPRGQLKNL KASYTLTEPQ LTAPLKKGQV VGTIDFQLNG KSIEQRPLIV MENVEEGGFF GRVWDFVMMK FHQWFGSWFS |
Length |
400 |
Mol. Wt |
43.609 kDa |
pI |
8.1 (calculated) |
Extinction coefficient |
55,920 - 56,045 (calc based on 8 Y, 8 W, and 1 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.
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Structure
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Structure figures<protect> | ||||||
Notes
Structures described by Chen et al (2009)[8]
Gene Product Resources
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
See Help:Gene_accessions for help with entering information into the Gene Accessions table.
Database | Accession | Notes |
---|---|---|
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
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Notes
Links
Name | URL | Comments |
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References
See Help:References for how to manage references in EcoliWiki.
- ↑ 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)
- ↑ 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
- ↑ Spratt, BG (1977) Properties of the penicillin-binding proteins of Escherichia coli K12,. Eur. J. Biochem. 72 341-52 PubMed
- ↑ 6.0 6.1 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
- ↑ 7.0 7.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed
- ↑ Chen, Y et al. (2009) Crystal structures of penicillin-binding protein 6 from Escherichia coli. J. Am. Chem. Soc. 131 14345-54 PubMed
Categories
- GO:0030288 ! outer membrane-bounded periplasmic space
- GO:0004180 ! carboxypeptidase activity
- GO:0005887 ! integral component of plasma membrane
- GO:0006508 ! proteolysis
- GO:0008360 ! regulation of cell shape
- GO:0009002 ! serine-type D-Ala-D-Ala carboxypeptidase activity
- GO:0009252 ! peptidoglycan biosynthetic process
- GO:0019898 ! extrinsic component of membrane
- Proteins