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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)DescriptionActionsGraphical viewLength
Metal bindingi16Copper 11
Metal bindingi19Copper 11
Metal bindingi84Copper 21
Metal bindingi87Copper 21
Active sitei4994-aspartylphosphate intermediateBy similarity1
Metal bindingi698MagnesiumPROSITE-ProRule annotation1
Metal bindingi702MagnesiumPROSITE-ProRule annotation1

GO - Molecular functioni

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.
BRENDAi3.6.3.54. 658.

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
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei162 – 181HelicalSequence analysisAdd BLAST20
Transmembranei196 – 218HelicalSequence analysisAdd BLAST23
Transmembranei230 – 249HelicalSequence analysisAdd BLAST20
Transmembranei259 – 278HelicalSequence analysisAdd BLAST20
Transmembranei412 – 434HelicalSequence analysisAdd BLAST23
Transmembranei447 – 469HelicalSequence analysisAdd BLAST23
Transmembranei756 – 775HelicalSequence analysisAdd BLAST20
Transmembranei779 – 796HelicalSequence analysisAdd BLAST18

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000463301 – 802Copper-exporting P-type ATPase AAdd BLAST802

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO32220.
PRIDEiO32220.

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 interactors.
MINTiMINT-8288686.
STRINGi224308.Bsubs1_010100018186.

Structurei

Secondary structure

1802
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 13Combined sources9
Helixi19 – 28Combined sources10
Beta strandi33 – 39Combined sources7
Helixi40 – 42Combined sources3
Beta strandi44 – 49Combined sources6
Turni51 – 53Combined sources3
Helixi56 – 66Combined sources11
Beta strandi69 – 71Combined sources3
Beta strandi73 – 81Combined sources9
Helixi85 – 96Combined sources12
Beta strandi101 – 103Combined sources3
Beta strandi108 – 117Combined sources10
Turni119 – 121Combined sources3
Helixi124 – 134Combined sources11
Beta strandi136 – 140Combined sources5
Beta strandi143 – 146Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO32220.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 72HMA 1PROSITE-ProRule annotationAdd BLAST67
Domaini74 – 140HMA 2PROSITE-ProRule annotationAdd BLAST67

Sequence similaritiesi

Contains 2 HMA domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C59. Bacteria.
COG2217. LUCA.
HOGENOMiHOG000250397.
InParanoidiO32220.
KOiK17686.
OMAiQAWVQAD.
PhylomeDBiO32220.

Family and domain databases

CDDicd00371. HMA. 2 hits.
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.
IPR006122. HMA_Cu_ion-bd.
IPR006121. HMA_dom.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 2 hits.
[Graphical view]
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.
WP_003242925.1. NZ_JNCM01000033.1.

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.
WP_003242925.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO32220. 2 interactors.
MINTiMINT-8288686.
STRINGi224308.Bsubs1_010100018186.

Protein family/group databases

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

Proteomic databases

PaxDbiO32220.
PRIDEiO32220.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105C59. Bacteria.
COG2217. LUCA.
HOGENOMiHOG000250397.
InParanoidiO32220.
KOiK17686.
OMAiQAWVQAD.
PhylomeDBiO32220.

Enzyme and pathway databases

BioCyciBSUB:BSU33500-MONOMER.
BRENDAi3.6.3.54. 658.

Miscellaneous databases

EvolutionaryTraceiO32220.

Family and domain databases

CDDicd00371. HMA. 2 hits.
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.
IPR006122. HMA_Cu_ion-bd.
IPR006121. HMA_dom.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 2 hits.
[Graphical view]
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...

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: November 30, 2016
This is version 158 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

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 one 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.