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UniProtKB/Swiss-Prot entry P32113

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name COPA_ENTHR
Primary accession number P32113
Secondary accession number Q47841
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on October 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 66)
Name and origin of the protein
Protein name Probable copper-importing P-type ATPase A
Synonym EC 3.6.3.-
Gene name
Name: copA
From
Enterococcus hirae [TaxID: 1354] 
Taxonomy Bacteria; Firmicutes; Lactobacillales; Enterococcaceae; Enterococcus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN COPPER HOMEOSTASIS.
STRAIN=ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459;
PubMed=8048974 [NCBI, ExPASy, EBI, Israel, Japan]
Odermatt A., Suter H., Krapf R., Solioz M.;
"Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae.";
J. Biol. Chem. 268:12775-12779(1993).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
STRAIN=ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459;
DOI=10.1074/jbc.270.9.4349; PubMed=7876197 [NCBI, ExPASy, EBI, Israel, Japan]
Odermatt A., Solioz M.;
"Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPases of Enterococcus hirae.";
J. Biol. Chem. 270:4349-4354(1995).
[3]
 INDUCTION BY COPPER AND SILVER.
STRAIN=ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459;
DOI=10.1006/bbrc.1994.1891; PubMed=8037745 [NCBI, ExPASy, EBI, Israel, Japan]
Odermatt A., Krapf R., Solioz M.;
"Induction of the putative copper ATPases, CopA and CopB, of Enterococcus hirae by Ag+ and Cu2+, and Ag+ extrusion by CopB.";
Biochem. Biophys. Res. Commun. 202:44-48(1994).
[4]
 INTERACTION WITH COPZ, AND MUTAGENESIS OF CYS-17 AND CYS-20.
STRAIN=ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459;
DOI=10.1006/bbrc.2001.5757; PubMed=11594769 [NCBI, ExPASy, EBI, Israel, Japan]
Multhaup G., Strausak D., Bissig K.-D., Solioz M.;
"Interaction of the CopZ copper chaperone with the CopA copper ATPase of Enterococcus hirae assessed by surface plasmon resonance.";
Biochem. Biophys. Res. Commun. 288:172-177(2001).
[5]
 FUNCTION AS A COPPER ATPASE, ACYLPHOSPHATE FORMATION, BIOPHYSICOCHEMICAL PROPERTIES, AND INHIBITION BY VANADATE.
STRAIN=ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459;
DOI=10.1006/bbrc.2000.4176; PubMed=11162579 [NCBI, ExPASy, EBI, Israel, Japan]
Wunderli-Ye H., Solioz M.;
"Purification and functional analysis of the copper ATPase CopA of Enterococcus hirae.";
Biochem. Biophys. Res. Commun. 280:713-719(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L13292; AAA61835.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z46807; CAA86837.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A45995; A45995.
3D structure databases
HSSP O32220; 1KQK. [HSSP ENTRY / PDB]
ModBase P32113.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0005507; Molecular function: copper ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004008; Molecular function: copper-exporting ATPase activity (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006825; Biological process: copper ion transport (inferred from electronic annotation from InterPro).
GO:0008152; Biological process: metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR006416; ATPase-IB_hvy.
IPR001757; ATPase_P.
IPR006403; ATPase_P_cat/Cu.
IPR001756; ATPase_P_Cu.
IPR005834; Dehalogen-like_hydro.
IPR008250; E1-E2_ATPase_reg.
IPR006121; HeavyMe_transpt.
Graphical view of domain structure.
PANTHER PTHR11939; ATPase_P; 1.
Pfam PF00122; E1-E2_ATPase; 1.
PF00403; HMA; 1.
PF00702; Hydrolase; 1.
Pfam graphical view of domain structure.
PRINTS PR00119; CATATPASE.
PR00943; CUATPASE.
TIGRFAMs TIGR01511; ATPase-IB1_Cu; 1.
TIGR01525; ATPase-IB_hvy; 1.
TIGR01494; ATPase_P-type; 2.
PROSITE PS00154; ATPASE_E1_E2; 1.
PS01047; HMA_1; 1.
PS50846; HMA_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P32113.
ProtoNet P32113.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cell membrane; Copper; Copper transport; Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   727  727     Probable copper-importing P-type ATPase A. PRO_0000046250
TOPO_DOM   1    94  94     Cytoplasmic (Potential). 
TRANSMEM   95   115  21     Potential. 
TOPO_DOM   116   119  4     Extracellular (Potential). 
TRANSMEM   120   137  18     Potential. 
TOPO_DOM   138   161  24     Cytoplasmic (Potential). 
TRANSMEM   162   181  20     Potential. 
TOPO_DOM   182   187  6     Extracellular (Potential). 
TRANSMEM   188   203  16     Potential. 
TOPO_DOM   204   341  138     Cytoplasmic (Potential). 
TRANSMEM   342   362  21     Potential. 
TOPO_DOM   363   375  13     Extracellular (Potential). 
TRANSMEM   376   396  21     Potential. 
TOPO_DOM   397   678  282     Cytoplasmic (Potential). 
TRANSMEM   679   698  20     Potential. 
TOPO_DOM   699   700  2     Extracellular (Potential). 
TRANSMEM   701   721  21     Potential. 
TOPO_DOM   722   727  6     Cytoplasmic (Potential). 
DOMAIN   7    71  65     HMA. 
ACT_SITE   425   425        4-aspartylphosphate intermediate (By similarity). 
METAL   17    17        Copper (Potential). 
METAL   20    20        Copper (Potential). 
METAL   621   621        Magnesium (By similarity). 
METAL   625   625        Magnesium (By similarity). 
MUTAGEN   17    17        C->S: Still strongly interacts with copZ but abolishes the modulating activity of copper; when associated with S-20. 
MUTAGEN   20    20        C->S: Still strongly interacts with copZ but abolishes the modulating activity of copper; when associated with S-17. 
Sequence information
Length: 727 AA [This is the length of the unprocessed precursor] Molecular weight: 78388 Da [This is the MW of the unprocessed precursor] CRC64: 9FB8D1476F0D7A7F [This is a checksum on the sequence] 
        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
P32113 in FASTA format

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