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O32220 (COPA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Copper-exporting P-type ATPase A

Short name=Protein CopA
EC=3.6.3.54
Alternative name(s):
Cu(+)-exporting ATPase
Gene names
Name:copA
Synonyms:yvgX
Ordered Locus Names:BSU33500
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length802 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in copper export. Ref.2

Catalytic activity

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

Subunit structure

Monomer at sub-stoichiometric copper concentrations. Homodimer at higher copper concentrations. Forms a heterodimer (electrostatic interactions) with CopZ during the transfer of Cu+. Ref.7

Subcellular location

Cell membrane; Multi-pass membrane protein.

Induction

By Cu2+. Ref.2 Ref.3

Miscellaneous

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

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]

Contains 2 HMA domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-905041,EBI-905041

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 802802Copper-exporting P-type ATPase A
PRO_0000046330

Regions

Transmembrane162 – 18120Helical; Potential
Transmembrane196 – 21823Helical; Potential
Transmembrane230 – 24920Helical; Potential
Transmembrane259 – 27820Helical; Potential
Transmembrane412 – 43423Helical; Potential
Transmembrane447 – 46923Helical; Potential
Transmembrane756 – 77520Helical; Potential
Transmembrane779 – 79618Helical; Potential
Domain6 – 7267HMA 1
Domain74 – 14067HMA 2

Sites

Active site49914-aspartylphosphate intermediate By similarity
Metal binding161Copper 1
Metal binding191Copper 1
Metal binding841Copper 2
Metal binding871Copper 2
Metal binding6981Magnesium By similarity
Metal binding7021Magnesium By similarity

Secondary structure

................................ 802
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O32220 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: 8D6EC2B203E11E38

FASTA80285,912
        10         20         30         40         50         60 
MSEQKEIAMQ VSGMTCAACA ARIEKGLKRM PGVTDANVNL ATETSNVIYD PAETGTAAIQ 

        70         80         90        100        110        120 
EKIEKLGYHV VTEKAEFDIE GMTCAACANR IEKRLNKIEG VANAPVNFAL ETVTVEYNPK 

       130        140        150        160        170        180 
EASVSDLKEA VDKLGYKLKL KGEQDSEAAA KKKEERKQTA RLIFSAVLSF PLLWAMVSHF 

       190        200        210        220        230        240 
TFTSFIWVPD IFLNPWMQFA LATPVQFLIG WPFYVGAYKA LRNKSANMDV LVALGTTAAY 

       250        260        270        280        290        300 
AYSLYLTFQS IGSHGHTDGL YYETSAILLT LILLGKLFET KAKGRSSDAI KKLMKLQAKT 

       310        320        330        340        350        360 
ATVVRDGQEQ IIPIDEVLVN DIVYVKPGER IPVDGEVVEG RSAVDESMIT GESLPVDKNP 

       370        380        390        400        410        420 
GDSVTGSTVN ANGFLKIKAV NVGKDTALSH IIKIVEEAQG SKAPIQRLAD QISGIFVPIV 

       430        440        450        460        470        480 
LGIAVLTFLI WYLWAAPGDF AEAISKFIAV LVIACPCALG LATPTSIMAG SGRAAEFGIL 

       490        500        510        520        530        540 
FKGGEHLEKT HRLDTIVLDK TGTVTNGKPR LTDAIPFGRF EEKDLLQFAA AAETGSEHPL 

       550        560        570        580        590        600 
GEAIIAGVKD KGLEIPKLTR FEAKVGAGIL AEAGGKSILV GTRKLMESEQ VEHGALLAQM 

       610        620        630        640        650        660 
EELEAEGKTV MLVSIDGEAA GLVAVADTIK DTSRKAVARL KELGLDVIMM TGDNRRTAEA 

       670        680        690        700        710        720 
IAKEAGIANI IAEVLPEQKA AEIARLQKEG RQTAMVGDGI NDAPALATAD IGMAIGTGTD 

       730        740        750        760        770        780 
IAMETADITL IRGDLNSIAD AIRMSRLTMK NIKQNLFWAL GYNSLGIPIA ALGFLAPWIA 

       790        800 
GAAMAFSSVS VVLNALRLQK VK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL009126 Genomic DNA. Translation: CAB15355.2.
PIRE70041.
RefSeqNP_391230.2. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JWWNMR-A71-156[»]
1KQKNMR-A72-146[»]
1OPZNMR-A2-71[»]
1OQ3NMR-A2-71[»]
1OQ6NMR-A2-71[»]
1P6TNMR-A2-146[»]
2RMLNMR-A2-146[»]
ProteinModelPortalO32220.
SMRO32220. Positions 1-146, 266-766.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO32220. 1 interaction.
MINTMINT-8288686.
STRING224308.BSU33500.

Protein family/group databases

TCDB3.A.3.5.18. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbO32220.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15355; CAB15355; BSU33500.
GeneID937985.
KEGGbsu:BSU33500.
PATRIC18978702. VBIBacSub10457_3514.

Organism-specific databases

GenoListBSU33500. [Micado]

Phylogenomic databases

eggNOGCOG2217.
HOGENOMHOG000250397.
KOK17686.
OrthoDBEOG6742RM.
PhylomeDBO32220.

Enzyme and pathway databases

BioCycBSUB:BSU33500-MONOMER.

Family and domain databases

Gene3D2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProIPR023299. 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]
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 2 hits.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF55008. SSF55008. 2 hits.
SSF56784. SSF56784. 2 hits.
TIGRFAMsTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
TIGR00003. TIGR00003. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 2 hits.
PS50846. HMA_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO32220.

Entry information

Entry nameCOPA_BACSU
AccessionPrimary (citable) accession number: O32220
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 16, 2009
Last modified: July 9, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList