copA:Gene Product(s): Difference between revisions

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|-
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!align=left |Standard name
!align=left {{table heading style}} |Standard name
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CopA  
CopA  
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!align=left |Synonyms
!align=left {{table heading style}} |Synonyms
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copper transporter<ref name='LIB:Riley_2006'/>, B0484<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, YbaR<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, CopA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>  
copper transporter<ref name='LIB:Riley_2006'/>, B0484<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, YbaR<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, CopA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>  
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!align=left |Product description
!align=left {{table heading style}} |Product description
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YbaR<ref name='LIB:EcoCyc10.6'/>; Cu<sup>+</sup>-exporting ATPase<ref name='LIB:EcoCyc11.1'/>
YbaR<ref name='LIB:EcoCyc10.6'/>; Cu<sup>+</sup>-exporting ATPase<ref name='LIB:EcoCyc11.1'/>
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Copper-, silver-translocating P-type ATPase efflux pump; involved in copper resistance; copper- and silver-inducible; regulated by copper-responsive CueR activator<ref name='LIB:EcoGene'/>
Copper-, silver-translocating P-type ATPase efflux pump; involved in copper resistance; copper- and silver-inducible; regulated by copper-responsive CueR activator<ref name='LIB:EcoGene'/>
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!align=left |EC number (for enzymes)
!align=left {{table heading style}} |EC number (for enzymes)
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[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.4 3.6.3.4]<ref name='LIB:Riley_2006'/>
[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.4 3.6.3.4]<ref name='LIB:Riley_2006'/>
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!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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!align=left |Sequence
!align=left {{table heading style}} |Sequence
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[http://biocyc.org/ECOLI/sequence-aa?object=G6260-MONOMER at EcoCyc]  
[http://biocyc.org/ECOLI/sequence-aa?object=G6260-MONOMER at EcoCyc]  
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AFIYNSIGIP VAAGILWPFT GTLLNPVVAG AAMALSSITV VSNANRLLRF KPKE</pre>  
AFIYNSIGIP VAAGILWPFT GTLLNPVVAG AAMALSSITV VSNANRLLRF KPKE</pre>  
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!align=left |Length
!align=left {{table heading style}} |Length
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834
834
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!align=left |Mol. Wt
!align=left {{table heading style}} |Mol. Wt
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87.872 kDa
87.872 kDa
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!align=left |pI
!align=left {{table heading style}} |pI
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5.4 (calculated)
5.4 (calculated)
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!align=left |Extinction coefficient
!align=left {{table heading style}} |Extinction coefficient
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69,900 - 70,650 (calc based on 10 Y, 10 W, and 6 C residues)
69,900 - 70,650 (calc based on 10 Y, 10 W, and 6 C residues)
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[http://www.uniprot.org/uniprot/Q59385#section_features UniProt:Q59385]  
[http://www.uniprot.org/uniprot/Q59385#section_features UniProt:Q59385]
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<beststructure>
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</beststructure>
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Revision as of 19:34, 23 February 2010

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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

CopA

Synonyms

copper transporter[1], B0484[2][1], YbaR[2][1], CopA[2][1]

Product description

YbaR[2]; Cu+-exporting ATPase[3]

Copper-, silver-translocating P-type ATPase efflux pump; involved in copper resistance; copper- and silver-inducible; regulated by copper-responsive CueR activator[4]

EC number (for enzymes)

3.6.3.4[1]

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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(s) Evidence Code with/from Aspect Notes Status
GO:0004008

copper-exporting ATPase activity

GO_REF:0000002
GO_REF:0000003

IEA: Inferred from Electronic Annotation

InterPro:IPR006403
EC:3.6.3.4

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0005375

copper ion transmembrane transporter activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0187

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0003824

catalytic activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005834

F

Seeded from EcoCyc [6]

complete

GO:0000287

magnesium ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0460

F

Seeded from EcoCyc [6]

complete

GO:0000166

nucleotide binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded from EcoCyc [6]

complete

GO:0016020

membrane

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR000695
InterPro:IPR001757
InterPro:IPR006403
InterPro:IPR008250
SP_KW:KW-0472

C

Seeded from EcoCyc [6]

complete

GO:0015992

proton transport

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000695

P

Seeded from EcoCyc 12.5 [5]

complete

GO:0005507

copper ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0186

F

Seeded from EcoCyc [6]

complete

GO:0005524

ATP binding

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR000695
InterPro:IPR001757
InterPro:IPR006403
InterPro:IPR008250
SP_KW:KW-0067

F

Seeded from EcoCyc [6]

complete

GO:0006810

transport

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR001757
SP_KW:KW-0813

P

Seeded from EcoCyc 12.5 [5]

complete

GO:0006811

ion transport

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0406

P

Seeded from EcoCyc [6]

complete

GO:0006825

copper ion transport

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0187

P

Seeded from EcoCyc 12.5 [5]

complete

GO:0008152

metabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005834

P

Seeded from EcoCyc [6]

complete

GO:0015662

ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000695
InterPro:IPR001757
InterPro:IPR006416

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0016021

integral to membrane

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR006416
SP_KW:KW-0812

C

Seeded from EcoCyc [6]

complete

GO:0016787

hydrolase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0378

F

Seeded from EcoCyc [6]

complete

GO:0046873

metal ion transmembrane transporter activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006403

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0016820

hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008250

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0030001

metal ion transport

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006121
InterPro:IPR006403
InterPro:IPR006416

P

Seeded from EcoCyc 12.5 [5]

complete

GO:0046872

metal ion binding

GO_REF:0000002
GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR006121
InterPro:IPR006403
SP_KW:KW-0479

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0031224

intrinsic to membrane

PMID:12351646[7]

IDA: Inferred from Direct Assay

C

Seeded from Riley et al 2006 [1].

CopA was purified from everted membrane vesicles (Fig. 6).

complete

GO:0005886

plasma membrane

GO_REF:0000004
GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_KW:KW-1003
SP_SL:SL-0039

C

Seeded from EcoCyc [6]

complete

GO:0006754

ATP biosynthetic process

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000695
InterPro:IPR001757
InterPro:IPR006403
InterPro:IPR006416
InterPro:IPR008250

P

Seeded from EcoCyc [6]

complete

GO:0015662

ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism

PMID:11167016[8]

IDA: Inferred from Direct Assay

F

Figure 2

complete

GO:0015662

ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism

PMID:12351646[7]

IDA: Inferred from Direct Assay

F

complete

GO:0006825

copper ion transport

PMID:10639134[9]

IMP: Inferred from Mutant Phenotype

P

Everted membrane vesicles prepared from a ΔcopA strain that expressed copA from a plasmid accumulated 64Cu. Accumulation required ATP.

complete

GO:0043682

copper-transporting ATPase activity

F

required field missing

GO:0016021

integral to membrane

PMID:11152613[10]

ISM: Inferred from Sequence Model

C

Predicted transmembrane domains shown below in the table of Domains/Motifs/Modification sites.

complete

GO:0010273

detoxification of copper ion

PMID:10639134[9]

IMP: Inferred from Mutant Phenotype

P

copA mutants are sensitive to copper ions.

complete

GO:0016887

ATPase activity

PMID:12351646[7]

IDA: Inferred from Direct Assay

F

Fig. 6 shows ATPase activity of CopA purified from membrane vesicles.

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

sdhA

PMID:16606699[11]

Experiment(s):EBI-1136866

Protein

glpD

PMID:16606699[11]

Experiment(s):EBI-1136866

Protein

ydcD

PMID:16606699[11]

Experiment(s):EBI-1136866

Protein

dnaK

PMID:16606699[11]

Experiment(s):EBI-1136866

Protein

groL

PMID:16606699[11]

Experiment(s):EBI-1136866

Protein

hflB

PMID:16606699[11]

Experiment(s):EBI-1136866
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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 Source Notes

plasma membrane

C-terminus localized in the cytoplasm with 8 predicted transmembrane domains

Daley et al. (2005) [12]

Inner Membrane

PMID:10639134[9]

EchoLocation:copA


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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.

Sequence

at EcoCyc 

MSQTIDLTLD GLSCGHCVKR VKESLEQRPD VEQADVSITE AHVTGTASAE QLIETIKQAG
YDASVSHPKA KPLAESSIPS EALTAVSEAL PAATADDDDS QQLLLSGMSC ASCVTRVQNA
LQSVPGVTQA RVNLAERTAL VMGSASPQDL VQAVEKAGYG AEAIEDDAKR RERQQETAVA
TMKRFRWQAI VALAVGIPVM VWGMIGDNMM VTADNRSLWL VIGLITLAVM VFAGGHFYRS
AWKSLLNGAA TMDTLVALGT GVAWLYSMSV NLWPQWFPME ARHLYYEASA MIIGLINLGH
MLEARARQRS SKALEKLLDL TPPTARLVTD EGEKSVPLAE VQPGMLLRLT TGDRVPVDGE
ITQGEAWLDE AMLTGEPIPQ QKGEGDSVHA GTVVQDGSVL FRASAVGSHT TLSRIIRMVR
QAQSSKPEIG QLADKISAVF VPVVVVIALV SAAIWYFFGP APQIVYTLVI ATTVLIIACP
CALGLATPMS IISGVGRAAE FGVLVRDADA LQRASTLDTV VFDKTGTLTE GKPQVVAVKT
FADVDEAQAL RLAAALEQGS SHPLARAILD KAGDMQLPQV NGFRTLRGLG VSGEAEGHAL
LLGNQALLNE QQVGTKAIEA EITAQASQGA TPVLLAVDGK AVALLAVRDP LRSDSVAALQ
RLHKAGYRLV MLTGDNPTTA NAIAKEAGID EVIAGVLPDG KAEAIKHLQS EGRQVAMVGD
GINDAPALAQ ADVGIAMGGG SDVAIETAAI TLMRHSLMGV ADALAISRAT LHNMKQNLLG
AFIYNSIGIP VAAGILWPFT GTLLNPVVAG AAMALSSITV VSNANRLLRF KPKE
Length

834

Mol. Wt

87.872 kDa

pI

5.4 (calculated)

Extinction coefficient

69,900 - 70,650 (calc based on 10 Y, 10 W, and 6 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

Initiator Methionine

1

Removed

UniProt:Q59385


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<motif_map/>

tmhmm.php?gene=copA&show=pic&.jpg
Click the image to view raw output from TMHMM.

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

Structures

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

Models

View models at:

edit table

Structure figures

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

Purification protocol

PMID:12351646[7]


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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

EcoCyc (EcoliWiki Page)

EcoCyc:G6260-MONOMER

SwissModel (EcoliWiki Page)

SwissModel:Q59385

UniProt (EcoliWiki Page)

UniProt:Q59385

PFAM (EcoliWiki Page)

PFAM:PF00403

RefSeq (EcoliWiki Page)

RefSeq:NP_415017


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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. ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  6. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  7. ↑ 7.0 7.1 7.2 7.3 Fan, B & Rosen, BP (2002) Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase. J. Biol. Chem. 277 46987-92 PubMed
  8. ↑ Petersen, C & Møller, LB (2000) Control of copper homeostasis in Escherichia coli by a P-type ATPase, CopA, and a MerR-like transcriptional activator, CopR. Gene 261 289-98 PubMed
  9. ↑ 9.0 9.1 9.2 Rensing, C et al. (2000) CopA: An Escherichia coli Cu(I)-translocating P-type ATPase. Proc. Natl. Acad. Sci. U.S.A. 97 652-6 PubMed
  10. ↑ Krogh, A et al. (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305 567-80 PubMed
  11. ↑ 11.0 11.1 11.2 11.3 11.4 11.5 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  12. ↑ Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed

Categories

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