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P32113 (COPA_ENTHR) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable copper-importing P-type ATPase A
EC=3.6.3.-
Gene names
Name:copA
OrganismEnterococcus hirae
Taxonomic identifier1354 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

Protein attributes

Sequence length727 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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) (TC 3.A.3) family. Type IB subfamily. [View classification]

Contains 1 HMA domain.

Biophysicochemical properties

Kinetic parameters:

KM=0.2 mM for ATP Ref.5

Vmax=0.15 µmol/min/mg enzyme

pH dependence:

Optimum pH is 6.25.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 727727Probable copper-importing P-type ATPase A
PRO_0000046250

Regions

Topological domain1 – 9494Cytoplasmic Potential
Transmembrane95 – 11521Helical; Potential
Topological domain116 – 1194Extracellular Potential
Transmembrane120 – 13718Helical; Potential
Topological domain138 – 16124Cytoplasmic Potential
Transmembrane162 – 18120Helical; Potential
Topological domain182 – 1876Extracellular Potential
Transmembrane188 – 20316Helical; Potential
Topological domain204 – 341138Cytoplasmic Potential
Transmembrane342 – 36221Helical; Potential
Topological domain363 – 37513Extracellular Potential
Transmembrane376 – 39621Helical; Potential
Topological domain397 – 678282Cytoplasmic Potential
Transmembrane679 – 69820Helical; Potential
Topological domain699 – 7002Extracellular Potential
Transmembrane701 – 72121Helical; Potential
Topological domain722 – 7276Cytoplasmic Potential
Domain7 – 7165HMA

Sites

Active site42514-aspartylphosphate intermediate By similarity
Metal binding171Copper Potential
Metal binding201Copper Potential
Metal binding6211Magnesium By similarity
Metal binding6251Magnesium By similarity

Experimental info

Mutagenesis171C → S: Still strongly interacts with CopZ but abolishes the modulating activity of copper; when associated with S-20. Ref.4
Mutagenesis201C → S: Still strongly interacts with CopZ but abolishes the modulating activity of copper; when associated with S-17. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P32113 [UniParc].

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

FASTA72778,388
        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

« Hide

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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L13292 Genomic DNA. Translation: AAA61835.1.
Z46807 Genomic DNA. Translation: CAA86837.1.
PIRA45995.

3D structure databases

ProteinModelPortalP32113.
ModBaseSearch...

Protein family/group databases

TCDB3.A.3.5.1. P-type ATPase (P-ATPase) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR006403. ATPase_P-typ_cat/Cu-transptr.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
IPR006416. ATPase_P-typ_heavy-metal.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
Gene3DG3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit.
G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00943. CUATPASE.
PR00942. CUATPASEI.
SUPFAMSSF56784. HAD-like_dom. 1 hit.
SSF55008. HeavyMe_transpt. 1 hit.
TIGRFAMsTIGR01511. ATPase-IB1_Cu. 1 hit.
TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOPA_ENTHR
AccessionPrimary (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: September 21, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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