ampC: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

AmpC

Synonyms

beta-lactamase/D-alanine carboxypeptidase[1], B4150[2][1], AmpA[2][1], AmpC[2][1] , ampA, ECK4146, JW4111, b4150

Product description

β-lactamase; penicillin resistance[2][3]

Intrinsic weak beta-lactamase activity; penicillin resistance; affects morphology; penicillin-binding protein[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:0008800

beta-lactamase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001586

F

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:0017001

antibiotic catabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001586

P

Seeded from EcoCyc (v14.0)

complete

GO:0008800

beta-lactamase activity

PMID:9324260[5]

IDA: Inferred from Direct Assay

F

complete

GO:0030288

outer membrane-bounded periplasmic space

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001586

C

Seeded from EcoCyc (v14.0)

complete

GO:0042597

periplasmic space

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0574

C

Seeded from EcoCyc (v14.0)

complete

GO:0042597

periplasmic space

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0200

C

Seeded from EcoCyc (v14.0)

complete

GO:0046677

response to antibiotic

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0046

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

dnaK

PMID:16606699[6]

Experiment(s):EBI-1147567
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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

Periplasm

PMID:6795623[7]

EchoLocation:ampC


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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 

MFKTTLCALL ITASCSTFAA PQQINDIVHR TITPLIEQQK IPGMAVAVIY QGKPYYFTWG
YADIAKKQPV TQQTLFELGS VSKTFTGVLG GDAIARGEIK LSDPTTKYWP ELTAKQWNGI
TLLHLATYTA GGLPLQVPDE VKSSSDLLRF YQNWQPAWAP GTQRLYANSS IGLFGALAVK
PSGLSFEQAM QTRVFQPLKL NHTWINVPPA EEKNYAWGYR EGKAVHVSPG ALDAEAYGVK
STIEDMARWV QSNLKPLDIN EKTLQQGIQL AQSRYWQTGD MYQGLGWEML DWPVNPDSII
NGSDNKIALA ARPVKAITPP TPAVRASWVH KTGATGGFGS YVAFIPEKEL GIVMLANKNY
PNPARVDAAW QILNALQ
Length

377

Mol. Wt

41.556 kDa

pI

9.1 (calculated)

Extinction coefficient

93,850 - 94,100 (calc based on 15 Y, 13 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

1-19

UniProt Manual:Signal Peptides

UniProt:P00811

Modification Site

80

phosphorylation site at S80

probability greater than 75%

PMID:17938405[8]

Domain

25..377

PF00144 Beta-lactamase

PMID:19920124[9]

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

Structures

<beststructure> gene=ampC 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:16131975

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:948669

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0013592

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P00811

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10040

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10040

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:948669

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000036

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0038

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 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. ↑ Henderson, TA et al. (1997) AmpC and AmpH, proteins related to the class C beta-lactamases, bind penicillin and contribute to the normal morphology of Escherichia coli. J. Bacteriol. 179 6112-21 PubMed
  6. ↑ Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  7. ↑ Jaurin, B & Grundström, T (1981) ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type. Proc. Natl. Acad. Sci. U.S.A. 78 4897-901 PubMed
  8. ↑ 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
  9. ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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