Copper-exporting P-type ATPase A - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot Q59385 (COPA_ECOLI)

Last modified November 25, 2008. Version 82. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Copper-exporting P-type ATPase A
EC=3.6.3.n1

Gene names

Name:	copA
Synonyms:	ybaR
Ordered Locus Names:	b0484, JW0473

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	834 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Involved in copper export. May also be involved in silver export.
Catalytic activity	ATP + H(2)O + Cu(1+)(In) = ADP + phosphate + Cu(1+)(Out).
Enzyme regulation	Phosphorylation is inhibited by vanadate and sensitive to KOH and hydroxylamine. Phosphorylation is Cu(+)-dependent.
Subcellular location	Cell membrane; Multi-pass membrane proteinProbable.
Induction	Transcriptionally regulated by cueR in response to Cu(+) or Ag(+) ions.
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IB subfamily. Contains 2 HMA domains.
Biophysicochemical properties	Kinetic parameters: K_M=1.5 µM for copper K_M=0.5 mM for ATP V_max=0.19 µmol/min/mg enzyme (in the presence of Cu(1+))

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Ontologies

Keywords
Biological process	Copper transport Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Repeat Transmembrane
Ligand	ATP-binding Copper Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	copper ion transport Inferred from electronic annotation. Source: UniProtKB-KW metabolic process Inferred from electronic annotation. Source: InterPro proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW copper-exporting ATPase activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 834

833

Copper-exporting P-type ATPase A

PRO_0000046320

Regions

Transmembrane

187 – 207

Potential

Transmembrane

218 – 238

Potential

Transmembrane

254 – 274

Potential

Transmembrane

284 – 304

Potential

Transmembrane

438 – 458

Potential

Transmembrane

464 – 484

Potential

Transmembrane

779 – 799

Potential

Transmembrane

801 – 821

Potential

Domain

4 – 65

HMA 1

Domain

100 – 163

HMA 2

Sites

Active site

523

4-aspartylphosphate intermediate Probable

Metal binding

Copper Potential

Metal binding

Copper Potential

Metal binding

110

Copper Potential

Metal binding

113

Copper Potential

Metal binding

720

Magnesium By similarity

Metal binding

724

Magnesium By similarity

Experimental info

Mutagenesis

8 – 150

143

Missing: Loss of activity

Mutagenesis

C → A: No effect

Mutagenesis

C → A: No effect

Mutagenesis

110

C → A: No effect

Mutagenesis

113

C → A: No effect

Mutagenesis

479

C → A: Loss of copper resistance, transport and phosphoenzyme formation

Mutagenesis

481

C → A or H: Loss of copper resistance, transport and phosphoenzyme formation

Sequence conflict

162 – 181

EAIED…TAVAT → KRLKMTLNAASASKKPPSLA in AAB02268. Ref.1

Sequence conflict

508

A → R in AAB02268. Ref.1

Sequence conflict

576

Q → R in AAB02268. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q59385-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: CF84A18FE208E6F6
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FASTA

834

87,873

        10         20         30         40         50         60 
MSQTIDLTLD GLSCGHCVKR VKESLEQRPD VEQADVSITE AHVTGTASAE QLIETIKQAG 

        70         80         90        100        110        120 
YDASVSHPKA KPLAESSIPS EALTAVSEAL PAATADDDDS QQLLLSGMSC ASCVTRVQNA 

       130        140        150        160        170        180 
LQSVPGVTQA RVNLAERTAL VMGSASPQDL VQAVEKAGYG AEAIEDDAKR RERQQETAVA 

       190        200        210        220        230        240 
TMKRFRWQAI VALAVGIPVM VWGMIGDNMM VTADNRSLWL VIGLITLAVM VFAGGHFYRS 

       250        260        270        280        290        300 
AWKSLLNGAA TMDTLVALGT GVAWLYSMSV NLWPQWFPME ARHLYYEASA MIIGLINLGH 

       310        320        330        340        350        360 
MLEARARQRS SKALEKLLDL TPPTARLVTD EGEKSVPLAE VQPGMLLRLT TGDRVPVDGE 

       370        380        390        400        410        420 
ITQGEAWLDE AMLTGEPIPQ QKGEGDSVHA GTVVQDGSVL FRASAVGSHT TLSRIIRMVR 

       430        440        450        460        470        480 
QAQSSKPEIG QLADKISAVF VPVVVVIALV SAAIWYFFGP APQIVYTLVI ATTVLIIACP 

       490        500        510        520        530        540 
CALGLATPMS IISGVGRAAE FGVLVRDADA LQRASTLDTV VFDKTGTLTE GKPQVVAVKT 

       550        560        570        580        590        600 
FADVDEAQAL RLAAALEQGS SHPLARAILD KAGDMQLPQV NGFRTLRGLG VSGEAEGHAL 

       610        620        630        640        650        660 
LLGNQALLNE QQVGTKAIEA EITAQASQGA TPVLLAVDGK AVALLAVRDP LRSDSVAALQ 

       670        680        690        700        710        720 
RLHKAGYRLV MLTGDNPTTA NAIAKEAGID EVIAGVLPDG KAEAIKHLQS EGRQVAMVGD 

       730        740        750        760        770        780 
GINDAPALAQ ADVGIAMGGG SDVAIETAAI TLMRHSLMGV ADALAISRAT LHNMKQNLLG 

       790        800        810        820        830 
AFIYNSIGIP VAAGILWPFT GTLLNPVVAG AAMALSSITV VSNANRLLRF KPKE

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Das S., Chuang E., Vulpe C., Goldman J., Gitschier J. Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Small genes/gene-products in Escherichia coli K-12." Wasinger V.C., Humphery-Smith I. FEMS Microbiol. Lett. 169:375-382(1998) [PubMed: 9868784] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11. Strain: K12.
[6]	"CopA: an Escherichia coli Cu(I)-translocating P-type ATPase." Rensing C., Fan B., Sharma R., Mitra B., Rosen B.P. Proc. Natl. Acad. Sci. U.S.A. 97:652-656(2000) [PubMed: 10639134] [Abstract] Cited for: CHARACTERIZATION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Control of copper homeostasis in Escherichia coli by a P-type ATPase, CopA, and a MerR-like transcriptional activator, CopR." Petersen C., Moeller L.B. Gene 261:289-298(2000) [PubMed: 11167016] [Abstract] Cited for: CHARACTERIZATION. Strain: K12.
[8]	"Escherichia coli CopA N-terminal Cys(X)(2)Cys motifs are not required for copper resistance or transport." Fan B., Grass G., Rensing C., Rosen B.P. Biochem. Biophys. Res. Commun. 286:414-418(2001) [PubMed: 11500054] [Abstract] Cited for: MUTAGENESIS OF CYS-14; CYS-17; CYS-110 AND CYS-113.
[9]	"Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase." Fan B., Rosen B.P. J. Biol. Chem. 277:46987-46992(2002) [PubMed: 12351646] [Abstract] Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, PHOSPHORYLATION, MUTAGENESIS OF CYS-479 AND CYS-481. Strain: K12.
[10]	"Measurement of cytoplasmic copper, silver, and gold with a lux biosensor shows copper and silver, but not gold, efflux by the CopA ATPase of Escherichia coli." Stoyanov J.V., Magnani D., Solioz M. FEBS Lett. 546:391-394(2003) [PubMed: 12832075] [Abstract] Cited for: FUNCTION IN SILVER EXPORT. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

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Cross-references

Sequence databases
	U58330 Genomic DNA. Translation: AAB02268.1. U82664 Genomic DNA. Translation: AAB40238.1. U00096 Genomic DNA. Translation: AAC73586.1. AP009048 Genomic DNA. Translation: BAE76263.1.
PIR	C64779.
RefSeq	AP_001133.1. NP_415017.1.
3D structure databases
HSSP	HSSP built from PDB template 1AFJ based on UniProtKB P04129.
ModBase	Search...
Genome annotation databases
GeneID	946106.
GenomeReviews	Gene locus b0484 in contig U00096_GR. Gene locus JW0473 in contig AP009048_GR.
KEGG	ecj:JW0473. eco:b0484.
Organism-specific databases
EchoBASE	EB3035.
EcoGene	EG13246. copA.
CMR	Search...
Phylogenomic databases
HOGENOM	Q59385.
Enzyme and pathway databases
BioCyc	EcoCyc:G6260-MON.
Family and domain databases
InterPro	IPR006416. ATPase-IB_hvy. IPR001757. ATPase_P. IPR006403. ATPase_P_cat/Cu. IPR005834. Dehalogen-like_hydro. IPR008250. E1-E2_ATPase_reg. IPR000695. H_ATPase. IPR006121. HeavyMe_transpt. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00403. HMA. 2 hits. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00120. HATPASE.
TIGRFAMs	TIGR01511. ATPase-IB1_Cu. 1 hit. TIGR01525. ATPase-IB_hvy. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. PS01047. HMA_1. 1 hit. PS50846. HMA_2. 2 hits. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

COPA_ECOLI

Accession

Primary (citable) accession number: Q59385
Secondary accession number(s): P78245, Q2MBU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 82 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents