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Protein

Probable copper-exporting P-type ATPase A

Gene

copA

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probably involved in copper and silver export.1 Publication

Catalytic activityi

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

Enzyme regulationi

Activated by Cu+ and Ag+ and inhibited by vanadate. Activated by CopZ in its Cu+-bound form.2 Publications

Kineticsi

Shows higher affinity for Cu+ compared with Ag+.

  1. KM=0.25 mM for ATP2 Publications
  1. Vmax=14.9 µmol/h/mg enzyme with Ag+ as substrate2 Publications
  2. Vmax=3.7 µmol/h/mg enzyme with Cu+ as substrate2 Publications

pH dependencei

Optimum pH is 6.1-6.5.2 Publications

Temperature dependencei

Optimum temperature is 75 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi27CopperPROSITE-ProRule annotation1
Metal bindingi30CopperPROSITE-ProRule annotation1
Active sitei4244-aspartylphosphate intermediateBy similarity1
Metal bindingi618MagnesiumPROSITE-ProRule annotation1
Metal bindingi622MagnesiumPROSITE-ProRule annotation1
Metal bindingi751CopperPROSITE-ProRule annotation1
Metal bindingi754CopperPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi457 – 462ATPSequence analysis6
Nucleotide bindingi490 – 501ATPSequence analysisAdd BLAST12

GO - Molecular functioni

GO - Biological processi

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

BRENDAi3.6.3.54. 414.
SABIO-RKO29777.

Protein family/group databases

TCDBi3.A.3.5.7. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable copper-exporting P-type ATPase A (EC:3.6.3.54)
Alternative name(s):
Cu(+)-exporting ATPase
Gene namesi
Name:copA
Synonyms:pacS
Ordered Locus Names:AF_0473
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
Proteomesi
  • UP000002199 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 101CytoplasmicSequence analysisAdd BLAST101
Transmembranei102 – 122HelicalSequence analysisAdd BLAST21
Topological domaini123 – 128ExtracellularSequence analysis6
Transmembranei129 – 149HelicalSequence analysisAdd BLAST21
Topological domaini150 – 159CytoplasmicSequence analysis10
Transmembranei160 – 180HelicalSequence analysisAdd BLAST21
Topological domaini181 – 186ExtracellularSequence analysis6
Transmembranei187 – 204HelicalSequence analysisAdd BLAST18
Topological domaini205 – 339CytoplasmicSequence analysisAdd BLAST135
Transmembranei340 – 360HelicalSequence analysisAdd BLAST21
Topological domaini361 – 364ExtracellularSequence analysis4
Transmembranei365 – 385HelicalSequence analysisAdd BLAST21
Topological domaini386 – 680CytoplasmicSequence analysisAdd BLAST295
Transmembranei681 – 701HelicalSequence analysisAdd BLAST21
Topological domaini702 – 704ExtracellularSequence analysis3
Transmembranei705 – 725HelicalSequence analysisAdd BLAST21
Topological domaini726 – 804CytoplasmicSequence analysisAdd BLAST79

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi27C → A: Reduction in ATPase activity; when associated with A-30. 2 Publications1
Mutagenesisi30C → A: Reduction in ATPase activity; when associated with A-27. 2 Publications1
Mutagenesisi380C → A: Abolishes activity. 2 Publications1
Mutagenesisi382C → A or S: Abolishes activity. 2 Publications1
Mutagenesisi751C → 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. 2 Publications1
Mutagenesisi754C → 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. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003506011 – 804Probable copper-exporting P-type ATPase AAdd BLAST804

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiO29777.

Interactioni

Subunit structurei

Interacts with CopZ probably in the CopZ Cu+-bound form.1 Publication

Protein-protein interaction databases

DIPiDIP-46021N.
STRINGi224325.AF0473.

Structurei

Secondary structure

1804
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi215 – 222Combined sources8
Beta strandi225 – 231Combined sources7
Beta strandi234 – 239Combined sources6
Helixi240 – 242Combined sources3
Beta strandi248 – 251Combined sources4
Beta strandi259 – 265Combined sources7
Beta strandi268 – 271Combined sources4
Helixi273 – 276Combined sources4
Beta strandi282 – 284Combined sources3
Beta strandi301 – 307Combined sources7
Helixi309 – 311Combined sources3
Helixi313 – 325Combined sources13
Beta strandi404 – 406Combined sources3
Helixi411 – 417Combined sources7
Beta strandi420 – 424Combined sources5
Helixi425 – 429Combined sources5
Beta strandi435 – 444Combined sources10
Helixi446 – 456Combined sources11
Turni457 – 459Combined sources3
Helixi463 – 474Combined sources12
Beta strandi485 – 488Combined sources4
Turni489 – 491Combined sources3
Beta strandi492 – 495Combined sources4
Beta strandi498 – 501Combined sources4
Helixi503 – 508Combined sources6
Helixi515 – 526Combined sources12
Beta strandi530 – 536Combined sources7
Beta strandi539 – 547Combined sources9
Helixi554 – 563Combined sources10
Beta strandi567 – 571Combined sources5
Helixi576 – 586Combined sources11
Beta strandi589 – 592Combined sources4
Helixi597 – 599Combined sources3
Helixi600 – 607Combined sources8
Turni608 – 610Combined sources3
Beta strandi613 – 617Combined sources5
Turni619 – 621Combined sources3
Helixi623 – 628Combined sources6
Beta strandi629 – 635Combined sources7
Beta strandi646 – 653Combined sources8
Helixi656 – 663Combined sources8
Beta strandi740 – 750Combined sources11
Helixi752 – 754Combined sources3
Helixi755 – 764Combined sources10
Beta strandi768 – 772Combined sources5
Beta strandi774 – 782Combined sources9
Helixi783 – 785Combined sources3
Helixi786 – 795Combined sources10
Beta strandi799 – 802Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B8EX-ray2.30A/B/C407-671[»]
2HC8X-ray1.65A214-325[»]
2VOYelectron microscopy18.00F214-326[»]
I410-663[»]
J432-549[»]
3A1CX-ray1.85A/B398-673[»]
3A1DX-ray1.85A/B398-673[»]
3A1EX-ray1.95A/B398-673[»]
3FRYX-ray2.00A/B736-804[»]
3J08electron microscopy-A/B93-737[»]
3J09electron microscopy-A/B15-737[»]
ProteinModelPortaliO29777.
SMRiO29777.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO29777.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 83HMA 1PROSITE-ProRule annotationAdd BLAST67
Domaini741 – 802HMA 2PROSITE-ProRule annotationAdd BLAST62

Sequence similaritiesi

Contains 2 HMA domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiarCOG01576. Archaea.
COG2217. LUCA.
KOiK17686.
OMAiMPGYNWI.

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. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O29777-1 [UniParc]FASTAAdd to basket

« Hide

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

KLRS
Length:804
Mass (Da):86,432
Last modified:January 1, 1998 - v1
Checksum:i610EB948C1D6B16F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB90763.1.
PIRiA69309.
RefSeqiWP_010877980.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB90763; AAB90763; AF_0473.
GeneIDi24794013.
KEGGiafu:AF_0473.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB90763.1.
PIRiA69309.
RefSeqiWP_010877980.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2B8EX-ray2.30A/B/C407-671[»]
2HC8X-ray1.65A214-325[»]
2VOYelectron microscopy18.00F214-326[»]
I410-663[»]
J432-549[»]
3A1CX-ray1.85A/B398-673[»]
3A1DX-ray1.85A/B398-673[»]
3A1EX-ray1.95A/B398-673[»]
3FRYX-ray2.00A/B736-804[»]
3J08electron microscopy-A/B93-737[»]
3J09electron microscopy-A/B15-737[»]
ProteinModelPortaliO29777.
SMRiO29777.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46021N.
STRINGi224325.AF0473.

Protein family/group databases

TCDBi3.A.3.5.7. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PRIDEiO29777.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB90763; AAB90763; AF_0473.
GeneIDi24794013.
KEGGiafu:AF_0473.

Phylogenomic databases

eggNOGiarCOG01576. Archaea.
COG2217. LUCA.
KOiK17686.
OMAiMPGYNWI.

Enzyme and pathway databases

BRENDAi3.6.3.54. 414.
SABIO-RKO29777.

Miscellaneous databases

EvolutionaryTraceiO29777.

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. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOPA_ARCFU
AccessioniPrimary (citable) accession number: O29777
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.