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Entry version 184 (13 Nov 2019)
Sequence version 1 (01 Oct 1994)
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Protein

Zinc/cadmium/lead-transporting P-type ATPase

Gene

zntA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Confers resistance to zinc, cadmium and lead (PubMed:9405611, PubMed:9364914, PubMed:9830000, PubMed:10660539, PubMed:17326661). Couples the hydrolysis of ATP with the export of zinc, cadmium or lead, with highest activity when the metals are present as metal-thiolate complexes (PubMed:9405611, PubMed:10660539, PubMed:17326661). Can also bind nickel, copper, cobalt and mercury (PubMed:10660539, PubMed:17326661).5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by orthovanadate.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=6.9 µM for Pb2+ (at 37 degrees Celsius and pH 7.0)1 Publication
  2. KM=6.1 µM for Pb2+ (at 37 degrees Celsius and pH 7.0)1 Publication
  3. KM=118 µM for Pb2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  4. KM=150 µM for Pb2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  5. KM=5.1 µM for Zn2+ (at 37 degrees Celsius and pH 7.0)2 Publications
  6. KM=109 µM for Zn2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  7. KM=105 µM for Zn2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  8. KM=3.1 µM for Cd2+ (at 37 degrees Celsius and pH 7.0)1 Publication
  9. KM=115 µM for Cd2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  10. KM=123 µM for Cd2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  11. KM=3.4 µM for Cu2+ (at 37 degrees Celsius and pH 7.0)1 Publication
  12. KM=85 µM for Cu2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  13. KM=2.1 µM for Ni2+ (at 37 degrees Celsius and pH 7.0)1 Publication
  14. KM=169 µM for Ni2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  15. KM=4.0 µM for Co2+ (at 37 degrees Celsius and pH 7.0)1 Publication
  16. KM=75 µM for Co2+-thiolate (at 37 degrees Celsius and pH 7.0)1 Publication
  1. Vmax=0.88 µmol/min/mg enzyme with Pb2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  2. Vmax=0.638 µmol/min/mg enzyme with Pb2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  3. Vmax=3.02 µmol/min/mg enzyme with Pb2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  4. Vmax=2.497 µmol/min/mg enzyme with Pb2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  5. Vmax=0.19 µmol/min/mg enzyme with Zn2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  6. Vmax=0.21 µmol/min/mg enzyme with Zn2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  7. Vmax=0.96 µmol/min/mg enzyme with Zn2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  8. Vmax=0.932 µmol/min/mg enzyme with Zn2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  9. Vmax=0.102 µmol/min/mg enzyme with Cd2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  10. Vmax=1.16 µmol/min/mg enzyme with Cd2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  11. Vmax=0.862 µmol/min/mg enzyme with Cd2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  12. Vmax=0.085 µmol/min/mg enzyme with Cu2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  13. Vmax=0.104 µmol/min/mg enzyme with Cu2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  14. Vmax=0.076 µmol/min/mg enzyme with Ni2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  15. Vmax=0.138 µmol/min/mg enzyme with Ni2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  16. Vmax=0.036 µmol/min/mg enzyme with Co2+ as substrate (at 37 degrees Celsius and pH 7.0)1 Publication
  17. Vmax=0.103 µmol/min/mg enzyme with Co2+-thiolate as substrate (at 37 degrees Celsius and pH 7.0)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi58Zinc 11 Publication1
Metal bindingi59Zinc 12 Publications1 Publication1
Metal bindingi62Zinc 12 Publications1 Publication1
Metal bindingi392Zinc 24 Publications1
Metal bindingi394Zinc 24 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei4364-aspartylphosphate intermediateBy similarity1
Metal bindingi436MagnesiumBy similarity1
Metal bindingi438Magnesium; via carbonyl oxygenBy similarity1
Metal bindingi628MagnesiumBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei693Important for metal transportBy similarity2 Publications1
Metal bindingi714Zinc 22 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Translocase
Biological processIon transport, Transport, Zinc transport
LigandATP-binding, Cadmium, Lead, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:YHHO-MONOMER
ECOL316407:JW3434-MONOMER
MetaCyc:YHHO-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P37617

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.A.3.6.2 the p-type atpase (p-atpase) superfamily

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Zinc/cadmium/lead-transporting P-type ATPaseCurated (EC:3.6.3.33 Publications, EC:7.2.2.-2 Publications, EC:7.2.2.123 Publications)
Alternative name(s):
Pb(II)/Cd(II)/Zn(II)-translocating ATPase1 Publication
Zn(2+)/Cd(2+)/Pb(2+) export ATPaseCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:zntA2 Publications
Synonyms:yhhO
Ordered Locus Names:b3469, JW3434
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 124CytoplasmicCuratedAdd BLAST124
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei125 – 145HelicalSequence analysisAdd BLAST21
Topological domaini146PeriplasmicCurated1
Transmembranei147 – 167HelicalSequence analysisAdd BLAST21
Topological domaini168 – 179CytoplasmicCuratedAdd BLAST12
Transmembranei180 – 197HelicalSequence analysisAdd BLAST18
Topological domaini198 – 202PeriplasmicCurated5
Transmembranei203 – 222HelicalSequence analysisAdd BLAST20
Topological domaini223 – 356CytoplasmicCuratedAdd BLAST134
Transmembranei357 – 377HelicalSequence analysisAdd BLAST21
Topological domaini378 – 383PeriplasmicCurated6
Transmembranei384 – 404HelicalSequence analysisAdd BLAST21
Topological domaini405 – 685CytoplasmicCuratedAdd BLAST281
Transmembranei686 – 702HelicalSequence analysisAdd BLAST17
Topological domaini703 – 707PeriplasmicCurated5
Transmembranei708 – 729HelicalSequence analysisAdd BLAST22
Topological domaini730 – 732Cytoplasmic1 Publication3

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutant exhibits hypersensitivity to zinc, cadmium, lead and, to a lesser extent, cobalt and nickel.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi59 – 62CAAC → AAAA: 2-3-fold decrease in ATPase activity. Binds metal ion only at the transmembrane site. 1 Publication4
Mutagenesisi59 – 62CAAC → SAAS: Reduces the ATPase activity by 50%. Reduces level of phosphorylation. 1 Publication4
Mutagenesisi392 – 394CPC → APA: Lack of ATPase activity. Binds metal ion only at the N-terminal site. 1 Publication3
Mutagenesisi392 – 394CPC → SPS: Lack of ATPase activity. Loss of zinc-stimulated phosphorylation. 1 Publication3
Mutagenesisi392C → A: Lack of activity. Cannot bind metal at the transmembrane site. Lack of phosphorylation with ATP. 1 Publication1
Mutagenesisi392C → H or S: Decrease in activity. Binds Zn(2+), Cd(2+), Ni(2+), Co(2+) and Cu(2+), but not Pb(2+). 1 Publication1
Mutagenesisi393P → A: Lack of activity with any metal. Cannot bind metal at the transmembrane site. Lack of phosphorylation with ATP. 1 Publication1
Mutagenesisi394C → A: Lack of activity. Cannot bind metal at the transmembrane site. Lack of phosphorylation with ATP. 1 Publication1
Mutagenesisi394C → H or S: Decrease in activity. Binds Zn(2+), Cd(2+), Ni(2+), Co(2+) and Cu(2+), but not Pb(2+). 1 Publication1
Mutagenesisi693K → N: Loss of zinc-stimulated ATPase activity. Poorly phosphorylated with ATP. 1 Publication1
Mutagenesisi714D → M: Shows high metal-independent ATPase activity. Poorly phosphorylated with ATP. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000463321 – 732Zinc/cadmium/lead-transporting P-type ATPaseAdd BLAST732

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P37617

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P37617

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P37617

PRoteomics IDEntifications database

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PRIDEi
P37617

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced by zinc.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
4262921, 26 interactors

Database of interacting proteins

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DIPi
DIP-12947N

Protein interaction database and analysis system

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IntActi
P37617, 8 interactors

STRING: functional protein association networks

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STRINGi
511145.b3469

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1732
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P37617

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P37617

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini49 – 113HMAPROSITE-ProRule annotationAdd BLAST65

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Has two high-affinity metal-binding sites, one in the N-terminal region and another in the transmembrane region. Both sites are able to access and bind metal ion independently of each other. The N-terminal metal-binding site is not strictly necessary for activity and metal selectivity, but is needed for maximal activity and may be involved in regulation. The metal-binding site in the transmembrane region is essential for activity of the pump.3 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG4105C59 Bacteria
COG2217 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000250399

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P37617

KEGG Orthology (KO)

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KOi
K01534

Database for complete collections of gene phylogenies

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PhylomeDBi
P37617

Family and domain databases

Conserved Domains Database

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CDDi
cd00371 HMA, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.1110.10, 1 hit
3.40.50.1000, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR023299 ATPase_P-typ_cyto_dom_N
IPR018303 ATPase_P-typ_P_site
IPR023298 ATPase_P-typ_TM_dom_sf
IPR008250 ATPase_P-typ_transduc_dom_A_sf
IPR036412 HAD-like_sf
IPR023214 HAD_sf
IPR017969 Heavy-metal-associated_CS
IPR006121 HMA_dom
IPR036163 HMA_dom_sf
IPR027256 P-typ_ATPase_IB
IPR001757 P_typ_ATPase

Pfam protein domain database

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Pfami
View protein in Pfam
PF00403 HMA, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00120 HATPASE

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55008 SSF55008, 1 hit
SSF56784 SSF56784, 1 hit
SSF81653 SSF81653, 1 hit
SSF81665 SSF81665, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01525 ATPase-IB_hvy, 1 hit
TIGR01494 ATPase_P-type, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00154 ATPASE_E1_E2, 1 hit
PS01047 HMA_1, 1 hit
PS50846 HMA_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P37617-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTPDNHGKK APQFAAFKPL TTVQNANDCC CDGACSSTPT LSENVSGTRY
60 70 80 90 100
SWKVSGMDCA ACARKVENAV RQLAGVNQVQ VLFATEKLVV DADNDIRAQV
110 120 130 140 150
ESALQKAGYS LRDEQAAEEP QASRLKENLP LITLIVMMAI SWGLEQFNHP
160 170 180 190 200
FGQLAFIATT LVGLYPIARQ ALRLIKSGSY FAIETLMSVA AIGALFIGAT
210 220 230 240 250
AEAAMVLLLF LIGERLEGWA ASRARQGVSA LMALKPETAT RLRKGEREEV
260 270 280 290 300
AINSLRPGDV IEVAAGGRLP ADGKLLSPFA SFDESALTGE SIPVERATGD
310 320 330 340 350
KVPAGATSVD RLVTLEVLSE PGASAIDRIL KLIEEAEERR APIERFIDRF
360 370 380 390 400
SRIYTPAIMA VALLVTLVPP LLFAASWQEW IYKGLTLLLI GCPCALVIST
410 420 430 440 450
PAAITSGLAA AARRGALIKG GAALEQLGRV TQVAFDKTGT LTVGKPRVTA
460 470 480 490 500
IHPATGISES ELLTLAAAVE QGATHPLAQA IVREAQVAEL AIPTAESQRA
510 520 530 540 550
LVGSGIEAQV NGERVLICAA GKHPADAFTG LINELESAGQ TVVLVVRNDD
560 570 580 590 600
VLGVIALQDT LRADAATAIS ELNALGVKGV ILTGDNPRAA AAIAGELGLE
610 620 630 640 650
FKAGLLPEDK VKAVTELNQH APLAMVGDGI NDAPAMKAAA IGIAMGSGTD
660 670 680 690 700
VALETADAAL THNHLRGLVQ MIELARATHA NIRQNITIAL GLKGIFLVTT
710 720 730
LLGMTGLWLA VLADTGATVL VTANALRLLR RR
Length:732
Mass (Da):76,840
Last modified:October 1, 1994 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i25476EA830786465
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U00039 Genomic DNA Translation: AAB18444.1
U00096 Genomic DNA Translation: AAC76494.1
AP009048 Genomic DNA Translation: BAE77824.1

Protein sequence database of the Protein Information Resource

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PIRi
S47688

NCBI Reference Sequences

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RefSeqi
NP_417926.1, NC_000913.3
WP_000106551.1, NZ_SSZK01000008.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

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EnsemblBacteriai
AAC76494; AAC76494; b3469
BAE77824; BAE77824; BAE77824

Database of genes from NCBI RefSeq genomes

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GeneIDi
947972

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ecj:JW3434
eco:b3469

Pathosystems Resource Integration Center (PATRIC)

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PATRICi
fig|1411691.4.peg.3256

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA Translation: AAB18444.1
U00096 Genomic DNA Translation: AAC76494.1
AP009048 Genomic DNA Translation: BAE77824.1
PIRiS47688
RefSeqiNP_417926.1, NC_000913.3
WP_000106551.1, NZ_SSZK01000008.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MWYNMR-A46-118[»]
1MWZNMR-A46-118[»]
SMRiP37617
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4262921, 26 interactors
DIPiDIP-12947N
IntActiP37617, 8 interactors
STRINGi511145.b3469

Protein family/group databases

TCDBi3.A.3.6.2 the p-type atpase (p-atpase) superfamily

Proteomic databases

EPDiP37617
jPOSTiP37617
PaxDbiP37617
PRIDEiP37617

Genome annotation databases

EnsemblBacteriaiAAC76494; AAC76494; b3469
BAE77824; BAE77824; BAE77824
GeneIDi947972
KEGGiecj:JW3434
eco:b3469
PATRICifig|1411691.4.peg.3256

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

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EchoBASEi
EB2129

Phylogenomic databases

eggNOGiENOG4105C59 Bacteria
COG2217 LUCA
HOGENOMiHOG000250399
InParanoidiP37617
KOiK01534
PhylomeDBiP37617

Enzyme and pathway databases

BioCyciEcoCyc:YHHO-MONOMER
ECOL316407:JW3434-MONOMER
MetaCyc:YHHO-MONOMER
SABIO-RKiP37617

Miscellaneous databases

EvolutionaryTraceiP37617

Protein Ontology

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PROi
PR:P37617

Family and domain databases

CDDicd00371 HMA, 1 hit
Gene3Di3.40.1110.10, 1 hit
3.40.50.1000, 1 hit
InterProiView protein in InterPro
IPR023299 ATPase_P-typ_cyto_dom_N
IPR018303 ATPase_P-typ_P_site
IPR023298 ATPase_P-typ_TM_dom_sf
IPR008250 ATPase_P-typ_transduc_dom_A_sf
IPR036412 HAD-like_sf
IPR023214 HAD_sf
IPR017969 Heavy-metal-associated_CS
IPR006121 HMA_dom
IPR036163 HMA_dom_sf
IPR027256 P-typ_ATPase_IB
IPR001757 P_typ_ATPase
PfamiView protein in Pfam
PF00403 HMA, 1 hit
PRINTSiPR00120 HATPASE
SUPFAMiSSF55008 SSF55008, 1 hit
SSF56784 SSF56784, 1 hit
SSF81653 SSF81653, 1 hit
SSF81665 SSF81665, 1 hit
TIGRFAMsiTIGR01525 ATPase-IB_hvy, 1 hit
TIGR01494 ATPase_P-type, 1 hit
PROSITEiView protein in PROSITE
PS00154 ATPASE_E1_E2, 1 hit
PS01047 HMA_1, 1 hit
PS50846 HMA_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiZNTA_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P37617
Secondary accession number(s): Q2M7D2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 13, 2019
This is version 184 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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