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O32220

- COPA_BACSU

UniProt

O32220 - COPA_BACSU

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Protein

Copper-exporting P-type ATPase A

Gene
copA, yvgX, BSU33500
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 intermediate By similarity
Metal bindingi698 – 6981Magnesium By similarity
Metal bindingi702 – 7021Magnesium By similarity

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
Complete GO annotation...

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

Topology

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

GO - Cellular componenti

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

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+.2 Publications

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+.1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiO32220.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 7267HMA 1Add
BLAST
Domaini74 – 14067HMA 2Add
BLAST

Sequence similaritiesi

Contains 2 HMA domains.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 140 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

Similar proteinsi