Lead, cadmium, zinc and mercury-transporting ATPase (P37617)

Identification
Name:Lead, cadmium, zinc and mercury-transporting ATPase
Synonyms:Not Available
Gene Name:zntA
Enzyme Class:
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:Involved in export of lead, cadmium, zinc and mercury
Cellular Location:Cell inner membrane; Multi-pass membrane protein
SMPDB Pathways:
KEGG Pathways:Not Available
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Zinc + 1.0Adenosine triphosphate + 1.0Water → 1.0ADP + 1.0Phosphate + 1.0Hydrogen ion
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0Zinc → 1.0ADP + 1.0Hydrogen ion + 1.0Phosphate + 1.0Zinc
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0Nickel → 1.0ADP + 1.0Hydrogen ion + 1.0Nickel + 1.0Phosphate
ReactionCard
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+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Cadmium + 1.0Water → 1.0ADP + 1.0Hydrogen ion + 1.0Phosphate + 1.0Cadmium
ReactionCard
1.0Thumb+1.0Thumb+1.0Cd(2+)(In) → 1.0Thumb+1.0Thumb+1.0Cd(2+)(Out)
1.0Adenosine triphosphate + 1.0Water + 1.0Cd(2+)(In) → 1.0ADP + 1.0Inorganic phosphate + 1.0Cd(2+)(Out)
ReactionCard
1.0Thumb+1.0Thumb+1.0Zn(2+)(In) → 1.0Thumb+1.0Thumb+1.0Zn(2+)(Out)
1.0Adenosine triphosphate + 1.0Water + 1.0Zn(2+)(In) → 1.0ADP + 1.0Inorganic phosphate + 1.0Zn(2+)(Out)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21194CadmiumMetaboCard
ECMDB00657CopperMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB21391NickelMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
ECMDB01303ZincMetaboCard
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
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
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:b3469
Gene OrientationClockwise
Centisome Percentage:77.69
Left Sequence End3604474
Right Sequence End3606672
Gene Sequence:
>2199 bp
ATGCCCGTTGCCCACGTTGCCTTGCCCGTTCCGCTTCCTCGTACCTTTGACTATCTGCTG
CCAGAAGGCATGACGGTTAAAGCTGGGTGTCGCGTGCGCGTGCCGTTTGGCAAACAGCAG
GAGCGCATCGGGATTGTGGTATCAGTTAGCGATGCCAGCGAACTGCCGCTCAATGAGCTA
AAAGCGGTAGTCGAAGTGCTGGATAGTGAGCCGGTGTTTACTCACTCCGTCTGGCGATTG
CTGCTATGGGCGGCAGATTACTATCATCATCCGATTGGCGATGTGCTGTTTCATGCCTTG
CCGATTTTACTACGCCAGGGGCGGCCTGCGGCGAACGCGCCGATGTGGTACTGGTTTGCC
ACTGAACAAGGCCAGGCGGTGGATCTGAACAGCCTGAAACGCTCCCCCAAGCAACAACAG
GCGCTGGCGGCGTTACGGCAAGGCAAAATCTGGCGCGACCAGGTCGCCACGCTCGAATTT
AATGATGCCGCGTTGCAGGCGCTACGCAAAAAAGGTCTGTGTGATTTAGCAAGTGAAACA
CCAGAGTTTAGCGACTGGCGAACGAACTATGCCGTTTCTGGTGAGCGGTTGCGATTGAAT
ACCGAACAGGCCACCGCCGTTGGCGCAATTCATAGCGCGGCAGATACTTTTTCTGCCTGG
CTGCTGGCGGGCGTTACCGGTTCCGGTAAAACGGAGGTTTATCTCAGCGTACTGGAAAAC
GTGCTCGCTCAGGGCAAACAGGCGCTGGTGATGGTGCCGGAAATCGGCCTGACACCGCAA
ACTATCGCCCGTTTTCGTGAACGTTTTAATGCCCCCGTGGAAGTTCTGCATTCCGGCCTG
AACGACAGCGAGCGTCTTTCGGCGTGGCTGAAAGCGAAAAATGGTGAGGCGGCGATTGTG
ATCGGCACCCGCTCCGCGCTGTTTACGCCGTTTAAAAATCTCGGCGTGATTGTCATTGAT
GAAGAGCACGACAGCTCCTACAAGCAGCAGGAAGGCTGGCGCTATCATGCCCGCGACCTG
GCGGTGTATCGTGCGCACAGCGAGCAAATCCCGATTATTCTTGGCTCCGCAACGCCCGCG
CTGGAAACGTTATGCAACGTCCAGCAGAAAAAATACCGCCTGCTGCGCCTGACCCGTCGG
GCAGGGAATGCGCGTCCGGCAATTCAACATGTGCTGGATTTAAAAGGTCAGAAGGTGCAG
GCAGGTCTGGCTCCGGCGTTAATCACTCGTATGCGCCAGCATTTACAGGCTGATAACCAG
GTCATTCTCTTTCTTAACCGCCGTGGCTTTGCGCCTGCACTGCTGTGCCACGACTGTGGC
TGGATTGCCGAATGCCCACGTTGCGATCACTACTACACGCTGCATCAGGCGCAGCACCAT
CTGCGCTGCCACCACTGTGACAGTCAGCGTCCGGTGCCGCGCCAGTGCCCTTCCTGCGGT
TCCACGCACCTGGTCCCCGTGGGGCTGGGCACCGAACAGCTTGAACAGACGCTCGCGCCG
TTGTTCCCCGGCGTGCCCATTTCTCGTATCGACCGCGATACCACCAGCCGCAAAGGGGCG
CTGGAACAGCAACTGGCAGAAGTACATCGCGGCGGCGCGCGGATTTTGATTGGTACACAA
ATGCTGGCGAAAGGTCACCATTTCCCGGATGTGACGCTGGTTGCATTACTGGACGTGGAC
GGCGCGCTGTTTTCTGCCGATTTTCGCTCGGCAGAGCGTTTCGCTCAGCTTTACACCCAG
GTCGCCGGTCGTGCCGGGCGTGCGGGTAAACAGGGCGAAGTGGTGCTGCAAACGCACCAT
CCGGAACATCCTCTGTTGCAAACGTTGCTCTATAAAGGCTACGACGCCTTTGCCGAACAG
GCGCTGGCTGAGCGGCGAATGATGCAGCTACCGCCGTGGACCAGCCATGTGATTGTGCGT
GCGGAAGATCATAACAATCAGCACGCGCCATTGTTCCTGCAACAACTGCGTAATCTGATC
CTCTCCAGCCCACTGGCAGACGAGAAACTGTGGGTTCTCGGTCCGGTTCCGGCTCTGGCA
CCTAAACGTGGCGGTCGCTGGCGCTGGCAGATATTGTTGCAGCACCCTTCCCGCGTGCGC
TTGCAACACATCATTAACGGTACGCTGGCGCTCATCAATACAATACCGGATTCCCGTAAG
GTGAAATGGGTGCTGGATGTTGATCCGATTGAGGGTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:732
Protein Molecular Weight:76839
Protein Theoretical pI:6
PDB File:1MWZ
Signaling Regions:
  • None
Transmembrane Regions:
  • 125-145
  • 192-212
  • 357-377
  • 384-404
  • 462-482
  • 633-653
  • 694-714
Protein Sequence:
>Lead, cadmium, zinc and mercury-transporting ATPase
MSTPDNHGKKAPQFAAFKPLTTVQNANDCCCDGACSSTPTLSENVSGTRYSWKVSGMDCA
ACARKVENAVRQLAGVNQVQVLFATEKLVVDADNDIRAQVESALQKAGYSLRDEQAAEEP
QASRLKENLPLITLIVMMAISWGLEQFNHPFGQLAFIATTLVGLYPIARQALRLIKSGSY
FAIETLMSVAAIGALFIGATAEAAMVLLLFLIGERLEGWAASRARQGVSALMALKPETAT
RLRKGEREEVAINSLRPGDVIEVAAGGRLPADGKLLSPFASFDESALTGESIPVERATGD
KVPAGATSVDRLVTLEVLSEPGASAIDRILKLIEEAEERRAPIERFIDRFSRIYTPAIMA
VALLVTLVPPLLFAASWQEWIYKGLTLLLIGCPCALVISTPAAITSGLAAAARRGALIKG
GAALEQLGRVTQVAFDKTGTLTVGKPRVTAIHPATGISESELLTLAAAVEQGATHPLAQA
IVREAQVAELAIPTAESQRALVGSGIEAQVNGERVLICAAGKHPADAFTGLINELESAGQ
TVVLVVRNDDVLGVIALQDTLRADAATAISELNALGVKGVILTGDNPRAAAAIAGELGLE
FKAGLLPEDKVKAVTELNQHAPLAMVGDGINDAPAMKAAAIGIAMGSGTDVALETADAAL
THNHLRGLVQMIELARATHANIRQNITIALGLKGIFLVTTLLGMTGLWLAVLADTGATVL
VTANALRLLRRR
References
External Links:
ResourceLink
Uniprot ID:P37617
Uniprot Name:ATZN_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676125
PDB ID:1MWZ
Ecogene ID:EG12215
Ecocyc:EG12215
ColiBase:b3469
Kegg Gene:b3469
EchoBASE ID:EB2129
CCDB:ATZN_ECOLI
BacMap:16131341
General Reference:
  • Banci, L., Bertini, I., Ciofi-Baffoni, S., Finney, L. A., Outten, C. E., O'Halloran, T. V. (2002). "A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118)." J Mol Biol 323:883-897. Pubmed: 12417201
  • Beard, S. J., Hashim, R., Membrillo-Hernandez, J., Hughes, M. N., Poole, R. K. (1997). "Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase." Mol Microbiol 25:883-891. Pubmed: 9364914
  • 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
  • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D., von Heijne, G. (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308:1321-1323. Pubmed: 15919996
  • 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
  • Rensing, C., Mitra, B., Rosen, B. P. (1997). "The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase." Proc Natl Acad Sci U S A 94:14326-14331. Pubmed: 9405611
  • Sharma, R., Rensing, C., Rosen, B. P., Mitra, B. (2000). "The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli." J Biol Chem 275:3873-3878. Pubmed: 10660539
  • Sofia, H. J., Burland, V., Daniels, D. L., Plunkett, G. 3rd, Blattner, F. R. (1994). "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Nucleic Acids Res 22:2576-2586. Pubmed: 8041620