Probable copper-importing P-type ATPase A

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Reviewed, UniProtKB/Swiss-Prot P32113 (COPA_ENTHR)

Last modified June 16, 2009. Version 71. 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:
Probable copper-importing P-type ATPase A
EC=3.6.3.-

Gene names

Name:

copA

Organism

Enterococcus hirae

Taxonomic identifier

1354 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

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Protein attributes

Sequence length	727 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Probably involved in copper import under copper limiting conditions. Ref.1 Ref.5
Catalytic activity	ATP + H₂O + Cu¹⁺(Out) = ADP + phosphate + Cu¹⁺(In).
Enzyme regulation	Inhibited by vanadate.
Subunit structure	Monomer. Interacts with the copper chaperone copZ. Ref.4
Subcellular location	Cell membrane; Multi-pass membrane protein.
Induction	By copper and silver. Ref.3
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IB subfamily. Contains 1 HMA domain.
biophysicochemical properties	Kinetic parameters: K_M=0.2 mM for ATP V_max=0.15 µmol/min/mg enzyme pH dependence: Optimum pH is 6.25.

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Ontologies

Keywords
Biological process	Copper transport Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Ligand	ATP-binding Copper Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro copper ion transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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

Chain

1 – 727

727

Probable copper-importing P-type ATPase A

PRO_0000046250

Regions

Topological domain

1 – 94

Cytoplasmic Potential

Transmembrane

95 – 115

Potential

Topological domain

116 – 119

Extracellular Potential

Transmembrane

120 – 137

Potential

Topological domain

138 – 161

Cytoplasmic Potential

Transmembrane

162 – 181

Potential

Topological domain

182 – 187

Extracellular Potential

Transmembrane

188 – 203

Potential

Topological domain

204 – 341

138

Cytoplasmic Potential

Transmembrane

342 – 362

Potential

Topological domain

363 – 375

Extracellular Potential

Transmembrane

376 – 396

Potential

Topological domain

397 – 678

282

Cytoplasmic Potential

Transmembrane

679 – 698

Potential

Topological domain

699 – 700

Extracellular Potential

Transmembrane

701 – 721

Potential

Topological domain

722 – 727

Cytoplasmic Potential

Domain

7 – 71

HMA

Sites

Active site

425

4-aspartylphosphate intermediate By similarity

Metal binding

Copper Potential

Metal binding

Copper Potential

Metal binding

621

Magnesium By similarity

Metal binding

625

Magnesium By similarity

Experimental info

Mutagenesis

C → S: Still strongly interacts with copZ but abolishes the modulating activity of copper; when associated with S-20. Ref.4

Mutagenesis

C → S: Still strongly interacts with copZ but abolishes the modulating activity of copper; when associated with S-17. Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

P32113-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 9FB8D1476F0D7A7F
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FASTA

727

78,388

        10         20         30         40         50         60 
MATNTKMETF VITGMTCANC SARIEKELNE QPGVMSATVN LATEKASVKY TDTTTERLIK 

        70         80         90        100        110        120 
SVENIGYGAI LYDEAHKQKI AEEKQTYLRK MKFDLIFSAI LTLPLMLAMI AMMLGSHGPI 

       130        140        150        160        170        180 
VSFFHLSLVQ LLFALPVQFY VGWRFYKGAY HALKTKAPNM DVLVAIGTSA AFALSIYNGF 

       190        200        210        220        230        240 
FPSHSHDLYF ESSSMIITLI LLGKYLEHTA KSKTGDAIKQ MMSLQTKTAQ VLRDGKEETI 

       250        260        270        280        290        300 
AIDEVMIDDI LVIRPGEQVP TDGRIIAGTS ALDESMLTGE SVPVEKKEKD MVFGGTINTN 

       310        320        330        340        350        360 
GLIQIQVSQI GKDTVLAQII QMVEDAQGSK APIQQIADKI SGIFVPIVLF LALVTLLVTG 

       370        380        390        400        410        420 
WLTKDWQLAL LHSVSVLVIA CPCALGLATP TAIMVGTGVG AHNGILIKGG EALEGAAHLN 

       430        440        450        460        470        480 
SIILDKTGTI TQGRPEVTDV IGPKEIISLF YSLEHASEHP LGKAIVAYGA KVGAKTQPIT 

       490        500        510        520        530        540 
DFVAHPGAGI SGTINGVHYF AGTRKRLAEM NLSFDEFQEQ ALELEQAGKT VMFLANEEQV 

       550        560        570        580        590        600 
LGMIAVADQI KEDAKQAIEQ LQQKGVDVFM VTGDNQRAAQ AIGKQVGIDS DHIFAEVLPE 

       610        620        630        640        650        660 
EKANYVEKLQ KAGKKVGMVG DGINDAPALR LADVGIAMGS GTDIAMETAD VTLMNSHLTS 

       670        680        690        700        710        720 
INQMISLSAA TLKKIKQNLF WAFIYNTIGI PFAAFGFLNP IIAGGAMAFS SISVLLNSLS 


LNRKTIK

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References

[1]	"Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae." Odermatt A., Suter H., Krapf R., Solioz M. J. Biol. Chem. 268:12775-12779(1993) [PubMed: 8048974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN COPPER HOMEOSTASIS. Strain: ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459.
[2]	"Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPases of Enterococcus hirae." Odermatt A., Solioz M. J. Biol. Chem. 270:4349-4354(1995) [PubMed: 7876197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9. Strain: ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459.
[3]	"Induction of the putative copper ATPases, CopA and CopB, of Enterococcus hirae by Ag+ and Cu2+, and Ag+ extrusion by CopB." Odermatt A., Krapf R., Solioz M. Biochem. Biophys. Res. Commun. 202:44-48(1994) [PubMed: 8037745] [Abstract] Cited for: INDUCTION BY COPPER AND SILVER. Strain: ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459.
[4]	"Interaction of the CopZ copper chaperone with the CopA copper ATPase of Enterococcus hirae assessed by surface plasmon resonance." Multhaup G., Strausak D., Bissig K.-D., Solioz M. Biochem. Biophys. Res. Commun. 288:172-177(2001) [PubMed: 11594769] [Abstract] Cited for: INTERACTION WITH COPZ, MUTAGENESIS OF CYS-17 AND CYS-20. Strain: ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459.
[5]	"Purification and functional analysis of the copper ATPase CopA of Enterococcus hirae." Wunderli-Ye H., Solioz M. Biochem. Biophys. Res. Commun. 280:713-719(2001) [PubMed: 11162579] [Abstract] Cited for: FUNCTION AS A COPPER ATPASE, ACYLPHOSPHATE FORMATION, BIOPHYSICOCHEMICAL PROPERTIES, INHIBITION BY VANADATE. Strain: ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459.

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Cross-references

Sequence databases
	L13292 Genomic DNA. Translation: AAA61835.1. Z46807 Genomic DNA. Translation: CAA86837.1.
PIR	A45995.
3D structure databases
HSSP	HSSP built from PDB template 1KQK based on UniProtKB O32220.
ModBase	Search...
Protein family/group databases
TCDB	3.A.3.5.1. P-type ATPase (P-ATPase) superfamily.
Enzyme and pathway databases
BRENDA	3.6.3.4. 39265.
Family and domain databases
InterPro	IPR001877. ATPase1_Cu-transp. IPR008250. ATPase_P-typ_ATPase-assoc-reg. IPR006403. ATPase_P-typ_cat/Cu-transptr. IPR001756. ATPase_P-typ_Cu-transptr. IPR006416. ATPase_P-typ_heavy-metal. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_phosphor_site. IPR005834. Dehalogen-like_hydro. IPR017969. Heavy-metal-associated_CS. IPR006121. HeavyMe_transpt. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00403. HMA. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00943. CUATPASE. PR00942. CUATPASEI.
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. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

COPA_ENTHR

Accession

Primary (citable) accession number: P32113
Secondary accession number(s): Q47841

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 71 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents