Copper-exporting P-type ATPase A (Q59385)

Identification
Name:Copper-exporting P-type ATPase A
Synonyms:Not Available
Gene Name:copA
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:Involved in copper export. May also be involved in silver export
Cellular Location:Cell membrane; Multi-pass membrane protein (Probable)
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
EcoCyc Reactions:
1.0Cu++1.0Thumb+1.0Thumb → 1.0Cu++1.0Thumb+1.0Thumb+1.0Thumb
1.0Cu+ + 1.0Water + 1.0Adenosine triphosphate → 1.0Cu+ + 1.0Phosphate + 1.0ADP + 1.0Hydrogen ion
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Copper + 1.0Water → 1.0ADP + 1.0Hydrogen ion + 1.0Phosphate + 1.0Copper
ReactionCard
1.0Thumb+1.0Thumb+1.0Cu(+)(In) → 1.0Thumb+1.0Thumb+1.0Cu(+)(Out)
1.0Adenosine triphosphate + 1.0Water + 1.0Cu(+)(In) → 1.0ADP + 1.0Inorganic phosphate + 1.0Cu(+)(Out)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB00657CopperMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
integral to membrane
intrinsic to membrane
membrane
membrane part
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
ATPase activity, coupled to transmembrane movement of ions
ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
binding
catalytic activity
cation binding
cation transmembrane transporter activity
copper ion transmembrane transporter activity
copper-exporting ATPase activity
copper-transporting ATPase activity
di-, tri-valent inorganic cation transmembrane transporter activity
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
inorganic cation transmembrane transporter activity
ion binding
ion transmembrane transporter activity
metal ion binding
metal ion transmembrane transporter activity
nucleoside binding
purine nucleoside binding
substrate-specific transmembrane transporter activity
transmembrane transporter activity
transporter activity
Process
ATP biosynthetic process
cation transport
cellular nitrogen compound metabolic process
establishment of localization
ion transport
metabolic process
metal ion transport
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
purine nucleoside triphosphate biosynthetic process
purine nucleotide biosynthetic process
purine nucleotide metabolic process
purine ribonucleoside triphosphate biosynthetic process
transport
Gene Properties
Blattner:b0484
Gene OrientationCounterclockwise
Centisome Percentage:10.95
Left Sequence End508099
Right Sequence End510603
Gene Sequence:
>2505 bp
ATGTCACAAACTATCGACCTGACCCTGGACGGCCTGTCCTGCGGTCACTGCGTTAAACGC
GTGAAAGAAAGTCTTGAACAGCGTCCGGATGTTGAGCAGGCGGATGTGTCTATCACTGAA
GCGCACGTTACCGGGACTGCCAGTGCAGAACAGCTGATCGAAACCATCAAACAAGCGGGT
TATGACGCATCTGTAAGCCACCCAAAGGCTAAACCGCTGGCGGAGTCATCAATCCCGTCG
GAAGCACTGACAGCGGTTTCTGAGGCGCTTCCGGCAGCGACCGCCGATGACGATGACAGC
CAGCAGTTGCTGCTGAGCGGCATGAGCTGCGCCAGCTGTGTCACCCGCGTACAAAATGCG
CTGCAAAGCGTACCGGGCGTCACTCAGGCACGGGTAAACCTGGCGGAGCGTACTGCGCTG
GTGATGGGCAGTGCCTCCCCACAAGATTTAGTGCAGGCGGTGGAAAAAGCGGGCTACGGC
GCGGAAGCGATTGAAGATGACGCTAAACGCCGCGAGCGCCAGCAAGAAACCGCCGTCGCT
ACGATGAAGCGCTTCCGCTGGCAGGCAATTGTCGCACTGGCGGTGGGTATCCCGGTGATG
GTCTGGGGGATGATCGGCGATAACATGATGGTCACCGCTGACAACCGCAGCCTGTGGTTG
GTTATCGGCCTGATAACCCTGGCAGTGATGGTTTTCGCCGGCGGCCATTTTTACCGCAGT
GCATGGAAAAGCCTGCTGAACGGTGCGGCGACGATGGATACGCTGGTGGCGCTGGGTACT
GGCGTGGCGTGGCTCTATTCGATGAGCGTCAACCTGTGGCCGCAGTGGTTCCCGATGGAA
GCGCGACATCTTTATTACGAAGCCAGCGCGATGATTATCGGTCTGATCAATCTCGGCCAT
ATGCTGGAAGCGCGCGCACGCCAGCGTTCTTCTAAGGCGCTGGAAAAGTTACTCGATTTA
ACCCCGCCGACGGCACGCCTGGTTACTGACGAAGGTGAAAAAAGCGTGCCTCTGGCAGAA
GTGCAGCCAGGTATGTTGCTGCGCCTGACGACCGGCGATCGCGTGCCGGTAGATGGCGAG
ATTACCCAGGGCGAAGCATGGCTGGATGAAGCGATGCTGACGGGCGAACCAATCCCGCAG
CAAAAAGGCGAAGGCGATAGCGTCCATGCCGGGACAGTGGTACAGGACGGCAGTGTGCTG
TTTCGTGCCAGTGCGGTTGGCAGCCATACTACGCTGTCACGAATCATTCGCATGGTGCGC
CAGGCCCAGAGCAGCAAGCCAGAAATCGGTCAGCTGGCGGATAAAATCTCAGCCGTATTT
GTGCCGGTAGTGGTGGTTATTGCGCTTGTCAGTGCGGCAATCTGGTATTTCTTTGGTCCG
GCACCGCAGATTGTCTATACCCTGGTGATTGCCACCACGGTACTGATTATTGCCTGTCCG
TGTGCGCTGGGGCTGGCGACGCCGATGTCGATTATTTCCGGCGTCGGGCGGGCGGCTGAG
TTTGGCGTGCTGGTGCGGGACGCTGACGCGCTGCAACGCGCCAGTACACTCGACACTGTA
GTGTTCGATAAAACCGGGACGCTGACTGAAGGGAAGCCGCAGGTTGTCGCAGTGAAAACA
TTTGCTGATGTTGATGAAGCGCAGGCATTGCGTCTGGCGGCGGCACTGGAGCAAGGTTCC
AGCCATCCGCTGGCACGAGCGATCCTCGATAAAGCAGGTGATATGCAGCTACCGCAGGTC
AACGGTTTCCGCACATTGCGCGGGCTGGGCGTGAGCGGTGAAGCTGAAGGTCATGCGTTA
TTGCTGGGCAATCAGGCGCTGTTAAATGAGCAACAGGTTGGTACCAAAGCTATCGAAGCG
GAGATTACTGCTCAGGCATCGCAAGGGGCAACGCCTGTGCTGCTGGCGGTTGACGGGAAA
GCGGTAGCCCTGCTGGCAGTACGCGATCCGTTGCGTAGTGATAGCGTGGCGGCGCTGCAA
CGCCTGCATAAAGCGGGATATCGTCTGGTGATGTTGACCGGGGATAACCCAACCACCGCC
AATGCGATCGCCAAAGAAGCAGGGATTGATGAGGTGATCGCCGGGGTGCTGCCGGACGGT
AAAGCCGAAGCGATCAAACATCTGCAAAGTGAAGGACGTCAGGTGGCAATGGTGGGCGAC
GGCATTAACGACGCGCCAGCGCTGGCTCAGGCGGATGTCGGCATTGCGATGGGTGGCGGC
AGTGATGTTGCCATTGAAACCGCGGCGATTACCCTGATGCGCCATAGCCTGATGGGCGTT
GCGGATGCGCTCGCTATTTCCCGCGCAACGCTGCACAACATGAAGCAGAACCTGCTCGGT
GCGTTTATCTACAACAGTATCGGTATTCCGGTCGCCGCCGGTATTTTGTGGCCGTTCACT
GGAACACTGCTTAACCCGGTAGTTGCCGGAGCGGCAATGGCGCTCTCGTCGATTACCGTA
GTGAGTAACGCCAACCGGTTGCTGCGGTTTAAACCGAAGGAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:834
Protein Molecular Weight:87872
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • 187-207
  • 218-238
  • 254-274
  • 284-304
  • 438-458
  • 464-484
  • 779-799
  • 801-821
Protein Sequence:
>Copper-exporting P-type ATPase A
MSQTIDLTLDGLSCGHCVKRVKESLEQRPDVEQADVSITEAHVTGTASAEQLIETIKQAG
YDASVSHPKAKPLAESSIPSEALTAVSEALPAATADDDDSQQLLLSGMSCASCVTRVQNA
LQSVPGVTQARVNLAERTALVMGSASPQDLVQAVEKAGYGAEAIEDDAKRRERQQETAVA
TMKRFRWQAIVALAVGIPVMVWGMIGDNMMVTADNRSLWLVIGLITLAVMVFAGGHFYRS
AWKSLLNGAATMDTLVALGTGVAWLYSMSVNLWPQWFPMEARHLYYEASAMIIGLINLGH
MLEARARQRSSKALEKLLDLTPPTARLVTDEGEKSVPLAEVQPGMLLRLTTGDRVPVDGE
ITQGEAWLDEAMLTGEPIPQQKGEGDSVHAGTVVQDGSVLFRASAVGSHTTLSRIIRMVR
QAQSSKPEIGQLADKISAVFVPVVVVIALVSAAIWYFFGPAPQIVYTLVIATTVLIIACP
CALGLATPMSIISGVGRAAEFGVLVRDADALQRASTLDTVVFDKTGTLTEGKPQVVAVKT
FADVDEAQALRLAAALEQGSSHPLARAILDKAGDMQLPQVNGFRTLRGLGVSGEAEGHAL
LLGNQALLNEQQVGTKAIEAEITAQASQGATPVLLAVDGKAVALLAVRDPLRSDSVAALQ
RLHKAGYRLVMLTGDNPTTANAIAKEAGIDEVIAGVLPDGKAEAIKHLQSEGRQVAMVGD
GINDAPALAQADVGIAMGGGSDVAIETAAITLMRHSLMGVADALAISRATLHNMKQNLLG
AFIYNSIGIPVAAGILWPFTGTLLNPVVAGAAMALSSITVVSNANRLLRFKPKE
References
External Links:
ResourceLink
Uniprot ID:Q59385
Uniprot Name:COPA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674623
Ecogene ID:EG13246
Ecocyc:EG13246
ColiBase:b0484
Kegg Gene:b0484
EchoBASE ID:EB3035
CCDB:COPA_ECOLI
BacMap:16128468
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Fan, B., Grass, G., Rensing, C., Rosen, B. P. (2001). "Escherichia coli CopA N-terminal Cys(X)(2)Cys motifs are not required for copper resistance or transport." Biochem Biophys Res Commun 286:414-418. Pubmed: 11500054
  • Fan, B., Rosen, B. P. (2002). "Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase." J Biol Chem 277:46987-46992. Pubmed: 12351646
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Petersen, C., Moller, L. B. (2000). "Control of copper homeostasis in Escherichia coli by a P-type ATPase, CopA, and a MerR-like transcriptional activator, CopR." Gene 261:289-298. Pubmed: 11167016
  • Rensing, C., Fan, B., Sharma, R., Mitra, B., Rosen, B. P. (2000). "CopA: An Escherichia coli Cu(I)-translocating P-type ATPase." Proc Natl Acad Sci U S A 97:652-656. Pubmed: 10639134
  • Stoyanov, J. V., Magnani, D., Solioz, M. (2003). "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." FEBS Lett 546:391-394. Pubmed: 12832075
  • Wasinger, V. C., Humphery-Smith, I. (1998). "Small genes/gene-products in Escherichia coli K-12." FEMS Microbiol Lett 169:375-382. Pubmed: 9868784