Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O32220

- COPA_BACSU

UniProt

O32220 - COPA_BACSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
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. 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.
InParanoidiO32220.
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 [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:
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.
InParanoidi O32220.
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: October 29, 2014
This is version 142 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