O29777 (COPA_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable copper-exporting P-type ATPase A
EC=3.6.3.n1

Gene names

Name:	copA
Synonyms:	pacS
Ordered Locus Names:	AF_0473

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	804 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probably involved in copper and silver export. Ref.2
Catalytic activity	ATP + H2O + Cu+(In) = ADP + phosphate + Cu+(Out). Ref.7
Enzyme regulation	Activated by Cu+ and Ag+ and inhibited by vanadate. Activated by CopZ in its Cu+-bound form. Ref.2 Ref.3
Subunit structure	Interacts with CopZ probably in the CopZ Cu+-bound form. Ref.5
Subcellular location	Cell membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification] Contains 2 HMA domains.
Biophysicochemical properties	Kinetic parameters: Shows higher affinity for Cu+ compared with Ag+. KM=0.25 mM for ATP Ref.2 Ref.3 Vmax=14.9 µmol/h/mg enzyme with Ag+ as substrate Vmax=3.7 µmol/h/mg enzyme with Cu+ as substrate pH dependence: Optimum pH is 6.1-6.5. Temperature dependence: Optimum temperature is 75 degrees Celsius.

Ontologies

Keywords
Biological process	Copper transport Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Copper Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure 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 ion binding Inferred from electronic annotation. Source: InterPro copper-exporting ATPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 804

804

Probable copper-exporting P-type ATPase A

PRO_0000350601

Regions

Topological domain

1 – 101

101

Cytoplasmic Potential

Transmembrane

102 – 122

21

Helical; Potential

Topological domain

123 – 128

6

Extracellular Potential

Transmembrane

129 – 149

21

Helical; Potential

Topological domain

150 – 159

10

Cytoplasmic Potential

Transmembrane

160 – 180

21

Helical; Potential

Topological domain

181 – 186

6

Extracellular Potential

Transmembrane

187 – 204

18

Helical; Potential

Topological domain

205 – 339

135

Cytoplasmic Potential

Transmembrane

340 – 360

21

Helical; Potential

Topological domain

361 – 364

4

Extracellular Potential

Transmembrane

365 – 385

21

Helical; Potential

Topological domain

386 – 680

295

Cytoplasmic Potential

Transmembrane

681 – 701

21

Helical; Potential

Topological domain

702 – 704

3

Extracellular Potential

Transmembrane

705 – 725

21

Helical; Potential

Topological domain

726 – 804

79

Cytoplasmic Potential

Domain

17 – 83

67

HMA 1

Domain

741 – 802

62

HMA 2

Nucleotide binding

457 – 462

6

ATP Potential

Nucleotide binding

490 – 501

12

ATP Potential

Sites

Active site

424

1

4-aspartylphosphate intermediate By similarity

Metal binding

27

1

Copper Potential

Metal binding

30

1

Copper Potential

Metal binding

618

1

Magnesium By similarity

Metal binding

622

1

Magnesium By similarity

Metal binding

751

1

Copper Potential

Metal binding

754

1

Copper Potential

Experimental info

Mutagenesis

27

1

C → A: Reduction in ATPase activity; when associated with A-30. Ref.3 Ref.4

Mutagenesis

30

1

C → A: Reduction in ATPase activity; when associated with A-27. Ref.3 Ref.4

Mutagenesis

380

1

C → A: Abolishes activity. Ref.3 Ref.4

Mutagenesis

382

1

C → A or S: Abolishes activity. Ref.3 Ref.4

Mutagenesis

751

1

C → A: No effect on ATPase activity; when associated with A-754. Reduction in ATPase activity; when associated with A-27; A-30 and A-754. Ref.3 Ref.4

Mutagenesis

754

1

C → A: No effect on ATPase activity, when associated with A-751. Reduction in ATPase activity; when associated with A-27; A-30 and A-751. Ref.3 Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

804

Helix Strand Turn

Details...

Helix

215 – 219

5

Beta strand

225 – 230

6

Beta strand

235 – 239

5

Helix

240 – 242

3

Beta strand

248 – 251

4

Beta strand

262 – 265

4

Beta strand

268 – 271

4

Beta strand

282 – 284

3

Beta strand

301 – 307

7

Helix

313 – 324

12

Sequences

	Sequence		Length	Mass (Da)
	O29777 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 610EB948C1D6B16F	FASTA	804	86,432
	10 20 30 40 50 60 MVKDTYISSA SKTPPMERTV RVTGMTCAMC VKSIETAVGS LEGVEEVRVN LATETAFIRF 70 80 90 100 110 120 DEKRIDFETI KRVIEDLGYG VVDEQAAVSA EVEHLSRMKR KLYVAAFAGV LLLFLAHFIS 130 140 150 160 170 180 LPYEDFVQLL IALPAIFYSG SSIFKAAFSA LRRRTLNMDV MYSMGVGAAF LASVLSTAGV 190 200 210 220 230 240 LPREYSFYET SVLLLAFLLL GRTLEARAKS RTGEAIKKLV GLQAKTAVVI RDGKEIAVPV 250 260 270 280 290 300 EEVAVGDIVI VRPGEKIPVD GVVVEGESYV DESMISGEPV PVLKSKGDEV FGATINNTGV 310 320 330 340 350 360 LKIRATRVGG ETLLAQIVKL VEDAMGSKPP IQRLADKVVA YFIPTVLLVA ISAFIYWYFI 370 380 390 400 410 420 AHAPLLFAFT TLIAVLVVAC PCAFGLATPT ALTVGMGKGA ELGILIKNAD ALEVAEKVTA 430 440 450 460 470 480 VIFDKTGTLT KGKPEVTDLV PLNGDERELL RLAAIAERRS EHPIAEAIVK KALEHGIELG 490 500 510 520 530 540 EPEKVEVIAG EGVVADGILV GNKRLMEDFG VAVSNEVELA LEKLEREAKT AVIVARNGRV 550 560 570 580 590 600 EGIIAVSDTL KESAKPAVQE LKRMGIKVGM ITGDNWRSAE AISRELNLDL VIAEVLPHQK 610 620 630 640 650 660 SEEVKKLQAK EVVAFVGDGI NDAPALAQAD LGIAVGSGSD VAVESGDIVL IRDDLRDVVA 670 680 690 700 710 720 AIQLSRKTMS KIKQNIFWAL IYNVILIPAA AGLLYPIFGV VFRPEFAGLA MAMSSVSVVA 730 740 750 760 770 780 NSLLLRNYVP PIRRGGDSVE KIVLELSGLS CHHCVARVKK ALEEAGAKVE KVDLNEAVVA 790 800 GNKEDVDKYI KAVEAAGYQA KLRS

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. , 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: 9389475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[2]	"Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the extremophile Archaeoglobus fulgidus." Mandal A.K., Cheung W.D., Arguello J.M. J. Biol. Chem. 277:7201-7208(2002) [PubMed: 11756450] [Abstract] Cited for: FUNCTION AS AN ATPASE, ENZYME REGULATION, INHIBITION BY VANADATE, BIOPHYSICOCHEMICAL PROPERTIES.
[3]	"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, MUTAGENESIS OF CYS-27; CYS-30; CYS-380; CYS-382; CYS-751 AND CYS-754.
[4]	"Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu(+)-ATPase CopA." Mandal A.K., Arguello J.M. Biochemistry 42:11040-11047(2003) [PubMed: 12974640] [Abstract] Cited for: MUTAGENESIS OF CYS-27; CYS-30; CYS-380; CYS-382; CYS-751 AND CYS-754.
[5]	"Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites." Gonzalez-Guerrero M., Arguello J.M. Proc. Natl. Acad. Sci. U.S.A. 105:5992-5997(2008) [PubMed: 18417453] [Abstract] Cited for: REGULATION, INTERACTION WITH COPZ.
[6]	"Structure of the actuator domain from the Archaeoglobus fulgidus Cu(+)-ATPase." Sazinsky M.H., Agarwal S., Arguello J.M., Rosenzweig A.C. Biochemistry 45:9949-9955(2006) [PubMed: 16906753] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 214-326.
[7]	"Structure of the ATP binding domain from the Archaeoglobus fulgidus Cu+-ATPase." Sazinsky M.H., Mandal A.K., Arguello J.M., Rosenzweig A.C. J. Biol. Chem. 281:11161-11166(2006) [PubMed: 16495228] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 407-671, CATALYTIC ACTIVITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000782 Genomic DNA. Translation: AAB90763.1.

PIR

A69309.

RefSeq

NP_069309.1. NC_000917.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B8E	X-ray	2.30	A/B/C	407-671	[»]
2HC8	X-ray	1.65	A	214-326	[»]
2VOY	electron microscopy	18.00	A	-	[»]
			F	214-326	[»]
			J	432-549	[»]
3A1C	X-ray	1.85	A/B	398-673	[»]
3A1D	X-ray	1.85	A/B	398-673	[»]
3A1E	X-ray	1.95	A/B	398-673	[»]
3FRY	X-ray	2.00	A/B	736-804	[»]
3J08	electron microscopy	-	A/B	93-737	[»]
3J09	electron microscopy	-	A/B	15-737	[»]

ProteinModelPortal

O29777.

SMR

O29777. Positions 214-326, 410-669.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46021N.

Protein family/group databases

TCDB

3.A.3.5.7. P-type ATPase (P-ATPase) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1483690.

GenomeReviews

Gene locus AF_0473 in contig AE000782_GR.

KEGG

afu:AF0473.

NMPDR

fig|224325.1.peg.468.

TIGR

AF_0473.

Phylogenomic databases

HOGENOM

HBG507745.

OMA

EESHDIE.

PhylomeDB

O29777.

Enzyme and pathway databases

BioCyc

AFUL224325:AF_0473-MONOMER.

BRENDA

3.6.3.4. 414.

Family and domain databases

InterPro

IPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR006403. ATPase_P-typ_cat/Cu-transptr.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
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.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
IPR006122. HMA_Cu_ion-bd.
[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.
PF00403. HMA. 2 hits.
PF00702. Hydrolase. 1 hit.
[Graphical view]

PRINTS

PR00119. CATATPASE.
PR00943. CUATPASE.

SUPFAM

SSF56784. HAD-like_dom. 1 hit.
SSF55008. HeavyMe_transpt. 2 hits.

TIGRFAMs

TIGR01511. ATPase-IB1_Cu. 1 hit.
TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
TIGR00003. TIGR00003. 1 hit.

PROSITE

PS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

COPA_ARCFU

Accession

Primary (citable) accession number: O29777

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	January 1, 1998
Last modified:	December 14, 2011
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program