Reviewed,
UniProtKB/Swiss-Prot P58341 (ATCU1_RHIME)
Last modified
November 3, 2009.
Version 65.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Copper-transporting ATPase 1 EC=3.6.3.4 | ||||||||
| Gene names |
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| Encoded on | Plasmid pSymA (megaplasmid 1) | ||||||||
| Organism | Rhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP] | ||||||||
| Taxonomic identifier | 382 [NCBI] | ||||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium |
Protein attributes
| Sequence length | 826 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Involved in copper transport By similarity. |
| Catalytic activity | ATP + H2O + Cu2+(In) = ADP + phosphate + Cu2+(Out). |
| Subcellular location | Cell membrane; Multi-pass membrane protein By similarity. |
| Sequence similarities | Belongs to the cation transport ATPase (P-type) family. Type IB subfamily. Contains 2 HMA domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Copper transport Ion transport Transport |
| Cellular component | Cell membrane Membrane |
| Domain | Repeat Transmembrane |
| Ligand | ATP-binding Copper Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Hydrolase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Plasmid |
| Gene Ontology (GO) | |
| Biological process | ATP biosynthetic process Inferred from electronic annotation. Source: InterPro copper ion transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW copper ion bindingInferred from electronic annotation. Source: UniProtKB-KW copper-exporting ATPase activityInferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 826 | 826 | Copper-transporting ATPase 1 | PRO_0000046327 | |||||
Regions | |||||||||
| Transmembrane | 172 – 192 | 21 | Potential | ||||||
| Transmembrane | 209 – 229 | 21 | Potential | ||||||
| Transmembrane | 246 – 266 | 21 | Potential | ||||||
| Transmembrane | 270 – 290 | 21 | Potential | ||||||
| Transmembrane | 429 – 449 | 21 | Potential | ||||||
| Transmembrane | 457 – 477 | 21 | Potential | ||||||
| Transmembrane | 772 – 792 | 21 | Potential | ||||||
| Transmembrane | 795 – 815 | 21 | Potential | ||||||
| Domain | 16 – 81 | 66 | HMA 1 | ||||||
| Domain | 83 – 148 | 66 | HMA 2 | ||||||
Sites | |||||||||
| Active site | 514 | 1 | 4-aspartylphosphate intermediate By similarity | ||||||
| Metal binding | 26 | 1 | Copper Potential | ||||||
| Metal binding | 29 | 1 | Copper Potential | ||||||
| Metal binding | 93 | 1 | Copper Potential | ||||||
| Metal binding | 96 | 1 | Copper Potential | ||||||
| Metal binding | 713 | 1 | Magnesium By similarity | ||||||
| Metal binding | 717 | 1 | Magnesium By similarity | ||||||
Sequences
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References
| [1] | "Nucleotide sequence and predicted functions of the entire Sinorhizobium meliloti pSymA megaplasmid." Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F., Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L., Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H. Long S.R.Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001) [PubMed: 11481432] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021. |
Cross-references
Sequence databases | |
|---|---|
| AE006469 Genomic DNA. Translation: AAK65206.1. | |
| PIR | D95330. |
| RefSeq | NP_435794.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JWW based on UniProtKB O32220. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1235584. |
| GenomeReviews | Gene locus RA0548 in contig AE006469_GR. |
| KEGG | sme:SMa1013. |
| NMPDR | fig|266834.1.peg.548. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P58341. |
| OMA | HEWIMEN. |
Enzyme and pathway databases | |
| BioCyc | SMEL266834:SMA1013-MON. |
| BRENDA | 3.6.3.4. 142. |
Family and domain databases | |
| InterPro | IPR008250. ATPase_P-typ_ATPase-assoc-reg. IPR006403. ATPase_P-typ_cat/Cu-transptr. IPR000695. ATPase_P-typ_H-transp. IPR006416. ATPase_P-typ_heavy-metal. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR006122. Cu_ion_bd. IPR005834. Dehalogen-like_hydro. IPR017969. Heavy-metal-associated_CS. IPR006121. HeavyMe_transpt. [Graphical view] |
| PANTHER | PTHR11939. ATPase_P. 1 hit. |
| Pfam | PF00122. E1-E2_ATPase. 1 hit. PF00403. HMA. 2 hits. PF00702. Hydrolase. 1 hit. [Graphical view] |
| PRINTS | PR00119. CATATPASE. PR00120. HATPASE. |
| TIGRFAMs | TIGR01511. ATPase-IB1_Cu. 1 hit. TIGR01525. ATPase-IB_hvy. 1 hit. TIGR01494. ATPase_P-type. 2 hits. TIGR00003. Cu_ion_bd. 2 hits. |
| PROSITE | PS00154. ATPASE_E1_E2. 1 hit. PS01047. HMA_1. 2 hits. PS50846. HMA_2. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ATCU1_RHIME | ||||||||
| Accession | Primary (citable) accession number: P58341 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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