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O30085 (COPB_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

EC=3.6.3.4
Gene names
Name:copB
Ordered Locus Names:AF_0152
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length690 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in copper export. Ref.3 Ref.4

Catalytic activity

ATP + H2O + Cu2+(Side 1) = ADP + phosphate + Cu2+(Side 2).

Enzyme regulation

Activated by Cu2+ and to a lesser extent by Ag+ and Cu+. Ref.2 Ref.3

Subcellular location

Cell membrane; Multi-pass membrane protein Potential.

Domain

The histidine-N-terminal metal-binding domain (His-N-MBD) seems to have a regulatory role affecting the metal transport rate by controlling the metal release/dephosphorylation rates.

Sequence similarities

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

Biophysicochemical properties

pH dependence:

Optimum pH is 5.7. Ref.2 Ref.3

Temperature dependence:

Optimum temperature is 85 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 690690Copper-exporting P-type ATPase B
PRO_0000350609

Regions

Topological domain1 – 6464Cytoplasmic Potential
Transmembrane65 – 8521Helical; Potential
Topological domain86 – 916Extracellular Potential
Transmembrane92 – 11221Helical; Potential
Topological domain113 – 12715Cytoplasmic Potential
Transmembrane128 – 14821Helical; Potential
Topological domain149 – 1513Extracellular Potential
Transmembrane152 – 17221Helical; Potential
Topological domain173 – 303131Cytoplasmic Potential
Transmembrane304 – 32421Helical; Potential
Topological domain325 – 33612Extracellular Potential
Transmembrane337 – 35721Helical; Potential
Topological domain358 – 640283Cytoplasmic Potential
Transmembrane641 – 66121Helical; Potential
Topological domain662 – 6632Extracellular Potential
Transmembrane664 – 68421Helical; Potential
Topological domain685 – 6906Cytoplasmic Potential
Region390 – 3912Phosphate binding
Region537 – 5382Phosphate binding
Compositional bias2 – 5150His-rich

Sites

Active site38914-aspartylphosphate intermediate Ref.4
Metal binding5831Magnesium By similarity
Metal binding5871Magnesium By similarity
Binding site5651Phosphate

Secondary structure

.................................................. 690
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O30085 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: AA063EF54B4F5EA2

FASTA69075,383
        10         20         30         40         50         60 
MHEHDSHGEA AHSNSEDMQM IHQHHEHHGH EEEHSAHHEK MKHSADHGDH HRMMMEDFKK 

        70         80         90        100        110        120 
RFYVSTLLTI PILILSPAIQ TFLGFRVEFA GSLYILFLLS SAVYFYGGYP FLKGIFDELR 

       130        140        150        160        170        180 
RRQPGMMTLI AVAISVAYFY SSAVVFGLKG KFFFWELATL IDIMLLGHYI EMRSVLGASR 

       190        200        210        220        230        240 
ALEELVKIMP SEAHLLKDGE IVEVKVENLK PGDKVLVKPG EKIPVDGIVV EGESFVNEAM 

       250        260        270        280        290        300 
LTGESKPVAK KPGDTVIGGA INGEGSLVVE VEKTGKDTYL NQVIELVRQA QESKSRTQDL 

       310        320        330        340        350        360 
ANRAALLLTV IALTVGSVTL AIWLAYIADF AFAIERAVTV MVITCPHALG LAIPLVVAVS 

       370        380        390        400        410        420 
TSLAAKSGLL IRDRQAFERA KDLQAVIFDK TGTLTEGRFG VTDIVGFNHS EDELLQIAAS 

       430        440        450        460        470        480 
LEARSEHPIA AAIVEEAEKR GFGLTEVEEF RAIPGKGVEG IVNGRRYMVV SPGYIRELGI 

       490        500        510        520        530        540 
KTDESVEKLK QQGKTVVFIL KNGEVSGVIA LADRIRPESR EAISKLKAIG IKCMMLTGDN 

       550        560        570        580        590        600 
RFVAKWVAEE LGLDDYFAEV LPHEKAEKVK EVQQKYVTAM VGDGVNDAPA LAQADVGIAI 

       610        620        630        640        650        660 
GAGTDVAVET ADIVLVRNDP RDVAAIVELS RKTYSKMKQN LLWATGYNAF AIPLAAGVLY 

       670        680        690 
SAGILLSPAV GAILMSLSTV IVAINARLLR 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. expand/collapse author list , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[2]"Heavy metal transport CPx-ATPases from the thermophile Archaeoglobus fulgidus."
Arguello J.M., Mandal A.K., Mana-Capelli S.
Ann. N. Y. Acad. Sci. 986:212-218(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, ATPASE ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[3]"Archaeoglobus fulgidus CopB is a thermophilic Cu2+-ATPase: functional role of its histidine-rich-N-terminal metal binding domain."
Mana-Capelli S., Mandal A.K., Arguello J.M.
J. Biol. Chem. 278:40534-40541(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A COPPER ATPASE, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[4]"Conformations of the apo-, substrate-bound and phosphate-bound ATP-binding domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to the catalytic cycle."
Jayakanthan S., Roberts S.A., Weichsel A., Arguello J.M., McEvoy M.M.
Biosci. Rep. 32:443-453(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 372-636 OF APOENZYME AND IN COMPLEX WITH PHOSPHATE, FUNCTION, ACTIVE SITE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000782 Genomic DNA. Translation: AAB91079.1.
PIRH69268.
RefSeqNP_068991.1. NC_000917.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3SKXX-ray1.59A372-636[»]
3SKYX-ray2.10A372-636[»]
ProteinModelPortalO30085.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224325.AF0152.

Protein family/group databases

TCDB3.A.3.5.10. the p-type atpase (p-atpase) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB91079; AAB91079; AF_0152.
GeneID1483363.
KEGGafu:AF0152.

Phylogenomic databases

eggNOGCOG2217.
KOK01533.
OMAFVFALER.

Enzyme and pathway databases

BioCycAFUL224325:GJBC-156-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.
[Graphical view]
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
SUPFAMSSF56784. SSF56784. 2 hits.
TIGRFAMsTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOPB_ARCFU
AccessionPrimary (citable) accession number: O30085
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 95 of the entry and version 1 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