Probable copper-exporting P-type ATPase B - Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)

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O30085 (COPB_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Probable copper-exporting P-type ATPase B
EC=3.6.3.4

Gene names

Name:	copB
Ordered Locus Names:	AF_0152

Organism

Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)

Taxonomic identifier

224325 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

Protein attributes

Sequence length	690 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probably involved in copper export. Ref.3
Catalytic activity	ATP + H₂O + Cu²⁺(In) = ADP + phosphate + Cu²⁺(Out).
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.

Ontologies

Keywords
Biological process	Copper transport Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Copper Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW copper-exporting ATPase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 690

690

Probable copper-exporting P-type ATPase B

PRO_0000350609

Regions

Topological domain

1 – 64

Cytoplasmic Potential

Transmembrane

65 – 85

Helical; Potential

Topological domain

86 – 91

Extracellular Potential

Transmembrane

92 – 112

Helical; Potential

Topological domain

113 – 127

Cytoplasmic Potential

Transmembrane

128 – 148

Helical; Potential

Topological domain

149 – 151

Extracellular Potential

Transmembrane

152 – 172

Helical; Potential

Topological domain

173 – 303

131

Cytoplasmic Potential

Transmembrane

304 – 324

Helical; Potential

Topological domain

325 – 336

Extracellular Potential

Transmembrane

337 – 357

Helical; Potential

Topological domain

358 – 640

283

Cytoplasmic Potential

Transmembrane

641 – 661

Helical; Potential

Topological domain

662 – 663

Extracellular Potential

Transmembrane

664 – 684

Helical; Potential

Topological domain

685 – 690

Cytoplasmic Potential

Compositional bias

2 – 51

His-rich

Sites

Active site

389

4-aspartylphosphate intermediate By similarity

Metal binding

583

Magnesium By similarity

Metal binding

587

Magnesium By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O30085 [UniParc].

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

690

75,383

        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' referencesShow '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. Venter J.C. Nature 390:364-370(1997) [PubMed: 9389475] [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: 12763798] [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: 12876283] [Abstract] Cited for: FUNCTION AS A COPPER ATPASE, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000782 Genomic DNA. Translation: AAB91079.1.
PIR	H69268.
RefSeq	NP_068991.1. NC_000917.1.
3D structure databases
ProteinModelPortal	O30085.
ModBase	Search...
Protein family/group databases
TCDB	3.A.3.5.10. P-type ATPase (P-ATPase) superfamily.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1483363.
GenomeReviews	Gene locus AF_0152 in contig AE000782_GR.
KEGG	afu:AF0152.
NMPDR	fig\|224325.1.peg.150.
TIGR	AF_0152.
Phylogenomic databases
HOGENOM	HBG507745.
OMA	EVLPHEK.
PhylomeDB	O30085.
Enzyme and pathway databases
BioCyc	AFUL224325:AF_0152-MONOMER.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR006403. ATPase_P-typ_cat/Cu-transptr. IPR006404. ATPase_P-typ_Cd/Co/Hg/Pb/Zn. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR000695. ATPase_P-typ_H-transp. IPR006416. ATPase_P-typ_heavy-metal. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit. G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KO	K01533.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00120. HATPASE.
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01511. ATPase-IB1_Cu. 1 hit. TIGR01512. ATPase-IB2_Cd. 1 hit. TIGR01525. ATPase-IB_hvy. 1 hit. TIGR01494. ATPase_P-type. 1 hit.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COPB_ARCFU

Accession

Primary (citable) accession number: O30085

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	January 1, 1998
Last modified:	December 14, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents