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O32220

- COPA_BACSU

UniProt

O32220 - COPA_BACSU

Protein

Copper-exporting P-type ATPase A

Gene

copA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    Involved in copper export.1 Publication

    Catalytic activityi

    ATP + H2O + Cu+(Side 1) = ADP + phosphate + Cu+(Side 2).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi16 – 161Copper 1
    Metal bindingi19 – 191Copper 1
    Metal bindingi84 – 841Copper 2
    Metal bindingi87 – 871Copper 2
    Active sitei499 – 49914-aspartylphosphate intermediateBy similarity
    Metal bindingi698 – 6981MagnesiumPROSITE-ProRule annotation
    Metal bindingi702 – 7021MagnesiumPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cation-transporting ATPase activity Source: InterPro
    3. copper ion binding Source: InterPro
    4. identical protein binding Source: IntAct

    GO - Biological processi

    1. copper ion transport Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Copper transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Copper, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU33500-MONOMER.

    Protein family/group databases

    TCDBi3.A.3.5.18. the p-type atpase (p-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Copper-exporting P-type ATPase A (EC:3.6.3.54)
    Short name:
    Protein CopA
    Alternative name(s):
    Cu(+)-exporting ATPase
    Gene namesi
    Name:copA
    Synonyms:yvgX
    Ordered Locus Names:BSU33500
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU33500. [Micado]

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 802802Copper-exporting P-type ATPase APRO_0000046330Add
    BLAST

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO32220.

    Expressioni

    Inductioni

    By Cu2+.1 Publication

    Interactioni

    Subunit structurei

    Monomer at sub-stoichiometric copper concentrations. Homodimer at higher copper concentrations. Forms a heterodimer (electrostatic interactions) with CopZ during the transfer of Cu+.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-905041,EBI-905041

    Protein-protein interaction databases

    IntActiO32220. 1 interaction.
    MINTiMINT-8288686.
    STRINGi224308.BSU33500.

    Structurei

    Secondary structure

    1
    802
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 139
    Helixi19 – 2810
    Beta strandi33 – 397
    Helixi40 – 423
    Beta strandi44 – 496
    Turni51 – 533
    Helixi56 – 6611
    Beta strandi69 – 713
    Beta strandi73 – 819
    Helixi85 – 9612
    Beta strandi101 – 1033
    Beta strandi108 – 11710
    Turni119 – 1213
    Helixi124 – 13411
    Beta strandi136 – 1405
    Beta strandi143 – 1464

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JWWNMR-A71-156[»]
    1KQKNMR-A72-146[»]
    1OPZNMR-A2-71[»]
    1OQ3NMR-A2-71[»]
    1OQ6NMR-A2-71[»]
    1P6TNMR-A2-146[»]
    2RMLNMR-A2-146[»]
    2VOYelectron microscopy18.00A71-146[»]
    ProteinModelPortaliO32220.
    SMRiO32220. Positions 1-146, 266-766.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO32220.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei162 – 18120HelicalSequence AnalysisAdd
    BLAST
    Transmembranei196 – 21823HelicalSequence AnalysisAdd
    BLAST
    Transmembranei230 – 24920HelicalSequence AnalysisAdd
    BLAST
    Transmembranei259 – 27820HelicalSequence AnalysisAdd
    BLAST
    Transmembranei412 – 43423HelicalSequence AnalysisAdd
    BLAST
    Transmembranei447 – 46923HelicalSequence AnalysisAdd
    BLAST
    Transmembranei756 – 77520HelicalSequence AnalysisAdd
    BLAST
    Transmembranei779 – 79618HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 7267HMA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini74 – 14067HMA 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 HMA domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2217.
    HOGENOMiHOG000250397.
    KOiK17686.
    OrthoDBiEOG6742RM.
    PhylomeDBiO32220.

    Family and domain databases

    Gene3Di2.70.150.10. 1 hit.
    3.40.1110.10. 1 hit.
    3.40.50.1000. 2 hits.
    InterProiIPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR027256. Cation_transp_P-typ_ATPase_IB.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    IPR017969. Heavy-metal-associated_CS.
    IPR006121. HeavyMe-assoc_HMA.
    IPR006122. HMA_Cu_ion-bd.
    [Graphical view]
    PfamiPF00122. E1-E2_ATPase. 1 hit.
    PF00403. HMA. 2 hits.
    PF00702. Hydrolase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    SUPFAMiSSF55008. SSF55008. 2 hits.
    SSF56784. SSF56784. 2 hits.
    TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
    TIGR01494. ATPase_P-type. 1 hit.
    TIGR00003. TIGR00003. 2 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    PS01047. HMA_1. 2 hits.
    PS50846. HMA_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O32220-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEQKEIAMQ VSGMTCAACA ARIEKGLKRM PGVTDANVNL ATETSNVIYD    50
    PAETGTAAIQ EKIEKLGYHV VTEKAEFDIE GMTCAACANR IEKRLNKIEG 100
    VANAPVNFAL ETVTVEYNPK EASVSDLKEA VDKLGYKLKL KGEQDSEAAA 150
    KKKEERKQTA RLIFSAVLSF PLLWAMVSHF TFTSFIWVPD IFLNPWMQFA 200
    LATPVQFLIG WPFYVGAYKA LRNKSANMDV LVALGTTAAY AYSLYLTFQS 250
    IGSHGHTDGL YYETSAILLT LILLGKLFET KAKGRSSDAI KKLMKLQAKT 300
    ATVVRDGQEQ IIPIDEVLVN DIVYVKPGER IPVDGEVVEG RSAVDESMIT 350
    GESLPVDKNP GDSVTGSTVN ANGFLKIKAV NVGKDTALSH IIKIVEEAQG 400
    SKAPIQRLAD QISGIFVPIV LGIAVLTFLI WYLWAAPGDF AEAISKFIAV 450
    LVIACPCALG LATPTSIMAG SGRAAEFGIL FKGGEHLEKT HRLDTIVLDK 500
    TGTVTNGKPR LTDAIPFGRF EEKDLLQFAA AAETGSEHPL GEAIIAGVKD 550
    KGLEIPKLTR FEAKVGAGIL AEAGGKSILV GTRKLMESEQ VEHGALLAQM 600
    EELEAEGKTV MLVSIDGEAA GLVAVADTIK DTSRKAVARL KELGLDVIMM 650
    TGDNRRTAEA IAKEAGIANI IAEVLPEQKA AEIARLQKEG RQTAMVGDGI 700
    NDAPALATAD IGMAIGTGTD IAMETADITL IRGDLNSIAD AIRMSRLTMK 750
    NIKQNLFWAL GYNSLGIPIA ALGFLAPWIA GAAMAFSSVS VVLNALRLQK 800
    VK 802
    Length:802
    Mass (Da):85,912
    Last modified:June 16, 2009 - v2
    Checksum:i8D6EC2B203E11E38
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB15355.2.
    PIRiE70041.
    RefSeqiNP_391230.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15355; CAB15355; BSU33500.
    GeneIDi937985.
    KEGGibsu:BSU33500.
    PATRICi18978702. VBIBacSub10457_3514.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB15355.2 .
    PIRi E70041.
    RefSeqi NP_391230.2. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JWW NMR - A 71-156 [» ]
    1KQK NMR - A 72-146 [» ]
    1OPZ NMR - A 2-71 [» ]
    1OQ3 NMR - A 2-71 [» ]
    1OQ6 NMR - A 2-71 [» ]
    1P6T NMR - A 2-146 [» ]
    2RML NMR - A 2-146 [» ]
    2VOY electron microscopy 18.00 A 71-146 [» ]
    ProteinModelPortali O32220.
    SMRi O32220. Positions 1-146, 266-766.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O32220. 1 interaction.
    MINTi MINT-8288686.
    STRINGi 224308.BSU33500.

    Protein family/group databases

    TCDBi 3.A.3.5.18. the p-type atpase (p-atpase) superfamily.

    Proteomic databases

    PaxDbi O32220.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15355 ; CAB15355 ; BSU33500 .
    GeneIDi 937985.
    KEGGi bsu:BSU33500.
    PATRICi 18978702. VBIBacSub10457_3514.

    Organism-specific databases

    GenoListi BSU33500. [Micado ]

    Phylogenomic databases

    eggNOGi COG2217.
    HOGENOMi HOG000250397.
    KOi K17686.
    OrthoDBi EOG6742RM.
    PhylomeDBi O32220.

    Enzyme and pathway databases

    BioCyci BSUB:BSU33500-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O32220.

    Family and domain databases

    Gene3Di 2.70.150.10. 1 hit.
    3.40.1110.10. 1 hit.
    3.40.50.1000. 2 hits.
    InterProi IPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR027256. Cation_transp_P-typ_ATPase_IB.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    IPR017969. Heavy-metal-associated_CS.
    IPR006121. HeavyMe-assoc_HMA.
    IPR006122. HMA_Cu_ion-bd.
    [Graphical view ]
    Pfami PF00122. E1-E2_ATPase. 1 hit.
    PF00403. HMA. 2 hits.
    PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    SUPFAMi SSF55008. SSF55008. 2 hits.
    SSF56784. SSF56784. 2 hits.
    TIGRFAMsi TIGR01525. ATPase-IB_hvy. 1 hit.
    TIGR01494. ATPase_P-type. 1 hit.
    TIGR00003. TIGR00003. 2 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    PS01047. HMA_1. 2 hits.
    PS50846. HMA_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    2. "CopZ from Bacillus subtilis interacts in vivo with a copper exporting CPx-type ATPase CopA."
      Radford D.S., Kihlken M.A., Borrelly G.P.M., Harwood C.R., Le Brun N.E., Cavet J.S.
      FEMS Microbiol. Lett. 220:105-112(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN COPPER EXPORT, INDUCTION BY COPPER, INTERACTION WITH COPZ.
      Strain: 168.
    3. "Two MerR homologues that affect copper induction of the Bacillus subtilis copZA operon."
      Gaballa A., Cao M., Helmann J.D.
      Microbiology 149:3413-3421(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REGULATION.
    4. "Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states."
      Banci L., Bertini I., Ciofi-Baffoni S., D'Onofrio M., Gonnelli L., Marhuenda-Egea F.C., Ruiz-Duenas F.J.
      J. Mol. Biol. 317:415-429(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-150 IN COMPLEX WITH COPPER IONS.
    5. "Structural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilis."
      Banci L., Bertini I., Ciofi-Baffoni S., Gonnelli L., Su X.-C.
      J. Biol. Chem. 278:50506-50513(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-150.
    6. "Understanding copper trafficking in bacteria: interaction between the copper transport protein CopZ and the N-terminal domain of the copper ATPase CopA from Bacillus subtilis."
      Banci L., Bertini I., Ciofi-Baffoni S., Del Conte R., Gonnelli L.
      Biochemistry 42:1939-1949(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-150.
    7. "Structure and Cu(I)-binding properties of the N-terminal soluble domains of Bacillus subtilis CopA."
      Singleton C., Banci L., Ciofi-Baffoni S., Tenori L., Kihlken M.A., Boetzel R., Le Brun N.E.
      Biochem. J. 411:571-579(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-146 IN COMPLEX WITH COPPER IONS, SUBUNIT.
      Strain: 168 / BGSC1A1.

    Entry informationi

    Entry nameiCOPA_BACSU
    AccessioniPrimary (citable) accession number: O32220
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 141 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The copZA operon is activated by CueR and indirectly repressed by YfmP.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3