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Protein

Copper-exporting P-type ATPase A

Gene

copA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: 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 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
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 – 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

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+.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. 2 interactions.
MINTiMINT-8288686.
STRINGi224308.BSU33500.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
InParanoidiO32220.
KOiK17686.
OMAiVNFALET.
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.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
IPR006122. HMA_Cu_ion-bd.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[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

        10         20         30         40         50
MSEQKEIAMQ VSGMTCAACA ARIEKGLKRM PGVTDANVNL ATETSNVIYD
60 70 80 90 100
PAETGTAAIQ EKIEKLGYHV VTEKAEFDIE GMTCAACANR IEKRLNKIEG
110 120 130 140 150
VANAPVNFAL ETVTVEYNPK EASVSDLKEA VDKLGYKLKL KGEQDSEAAA
160 170 180 190 200
KKKEERKQTA RLIFSAVLSF PLLWAMVSHF TFTSFIWVPD IFLNPWMQFA
210 220 230 240 250
LATPVQFLIG WPFYVGAYKA LRNKSANMDV LVALGTTAAY AYSLYLTFQS
260 270 280 290 300
IGSHGHTDGL YYETSAILLT LILLGKLFET KAKGRSSDAI KKLMKLQAKT
310 320 330 340 350
ATVVRDGQEQ IIPIDEVLVN DIVYVKPGER IPVDGEVVEG RSAVDESMIT
360 370 380 390 400
GESLPVDKNP GDSVTGSTVN ANGFLKIKAV NVGKDTALSH IIKIVEEAQG
410 420 430 440 450
SKAPIQRLAD QISGIFVPIV LGIAVLTFLI WYLWAAPGDF AEAISKFIAV
460 470 480 490 500
LVIACPCALG LATPTSIMAG SGRAAEFGIL FKGGEHLEKT HRLDTIVLDK
510 520 530 540 550
TGTVTNGKPR LTDAIPFGRF EEKDLLQFAA AAETGSEHPL GEAIIAGVKD
560 570 580 590 600
KGLEIPKLTR FEAKVGAGIL AEAGGKSILV GTRKLMESEQ VEHGALLAQM
610 620 630 640 650
EELEAEGKTV MLVSIDGEAA GLVAVADTIK DTSRKAVARL KELGLDVIMM
660 670 680 690 700
TGDNRRTAEA IAKEAGIANI IAEVLPEQKA AEIARLQKEG RQTAMVGDGI
710 720 730 740 750
NDAPALATAD IGMAIGTGTD IAMETADITL IRGDLNSIAD AIRMSRLTMK
760 770 780 790 800
NIKQNLFWAL GYNSLGIPIA ALGFLAPWIA GAAMAFSSVS VVLNALRLQK

VK
Length:802
Mass (Da):85,912
Last modified:June 16, 2009 - v2
Checksum:i8D6EC2B203E11E38
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15355.2.
PIRiE70041.
RefSeqiNP_391230.2. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

IntActiO32220. 2 interactions.
MINTiMINT-8288686.
STRINGi224308.BSU33500.

Protein family/group databases

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

Proteomic databases

PaxDbiO32220.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GenoListiBSU33500. [Micado]

Phylogenomic databases

eggNOGiCOG2217.
HOGENOMiHOG000250397.
InParanoidiO32220.
KOiK17686.
OMAiVNFALET.
OrthoDBiEOG6742RM.
PhylomeDBiO32220.

Enzyme and pathway databases

BioCyciBSUB:BSU33500-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO32220.

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.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
IPR006122. HMA_Cu_ion-bd.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[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]
ProtoNetiSearch...

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: January 7, 2015
This is version 144 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.