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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi27 – 271CopperPROSITE-ProRule annotation
Metal bindingi30 – 301CopperPROSITE-ProRule annotation
Active sitei424 – 42414-aspartylphosphate intermediateBy similarity
Metal bindingi618 – 6181MagnesiumPROSITE-ProRule annotation
Metal bindingi622 – 6221MagnesiumPROSITE-ProRule annotation
Metal bindingi751 – 7511CopperPROSITE-ProRule annotation
Metal bindingi754 – 7541CopperPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi457 – 4626ATPSequence analysis
Nucleotide bindingi490 – 50112ATPSequence analysisAdd
BLAST

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

BioCyciAFUL224325:GJBC-486-MONOMER.
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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 101101CytoplasmicSequence analysisAdd
BLAST
Transmembranei102 – 12221HelicalSequence analysisAdd
BLAST
Topological domaini123 – 1286ExtracellularSequence analysis
Transmembranei129 – 14921HelicalSequence analysisAdd
BLAST
Topological domaini150 – 15910CytoplasmicSequence analysis
Transmembranei160 – 18021HelicalSequence analysisAdd
BLAST
Topological domaini181 – 1866ExtracellularSequence analysis
Transmembranei187 – 20418HelicalSequence analysisAdd
BLAST
Topological domaini205 – 339135CytoplasmicSequence analysisAdd
BLAST
Transmembranei340 – 36021HelicalSequence analysisAdd
BLAST
Topological domaini361 – 3644ExtracellularSequence analysis
Transmembranei365 – 38521HelicalSequence analysisAdd
BLAST
Topological domaini386 – 680295CytoplasmicSequence analysisAdd
BLAST
Transmembranei681 – 70121HelicalSequence analysisAdd
BLAST
Topological domaini702 – 7043ExtracellularSequence analysis
Transmembranei705 – 72521HelicalSequence analysisAdd
BLAST
Topological domaini726 – 80479CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271C → A: Reduction in ATPase activity; when associated with A-30. 2 Publications
Mutagenesisi30 – 301C → A: Reduction in ATPase activity; when associated with A-27. 2 Publications
Mutagenesisi380 – 3801C → A: Abolishes activity. 2 Publications
Mutagenesisi382 – 3821C → A or S: Abolishes activity. 2 Publications
Mutagenesisi751 – 7511C → 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 Publications
Mutagenesisi754 – 7541C → 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 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 804804Probable copper-exporting P-type ATPase APRO_0000350601Add
BLAST

Keywords - PTMi

Phosphoprotein

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

1
804
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi215 – 2228Combined sources
Beta strandi225 – 2317Combined sources
Beta strandi234 – 2396Combined sources
Helixi240 – 2423Combined sources
Beta strandi248 – 2514Combined sources
Beta strandi259 – 2657Combined sources
Beta strandi268 – 2714Combined sources
Helixi273 – 2764Combined sources
Beta strandi282 – 2843Combined sources
Beta strandi301 – 3077Combined sources
Helixi309 – 3113Combined sources
Helixi313 – 32513Combined sources
Beta strandi404 – 4063Combined sources
Helixi411 – 4177Combined sources
Beta strandi420 – 4245Combined sources
Helixi425 – 4295Combined sources
Beta strandi435 – 44410Combined sources
Helixi446 – 45611Combined sources
Turni457 – 4593Combined sources
Helixi463 – 47412Combined sources
Beta strandi485 – 4884Combined sources
Turni489 – 4913Combined sources
Beta strandi492 – 4954Combined sources
Beta strandi498 – 5014Combined sources
Helixi503 – 5086Combined sources
Helixi515 – 52612Combined sources
Beta strandi530 – 5367Combined sources
Beta strandi539 – 5479Combined sources
Helixi554 – 56310Combined sources
Beta strandi567 – 5715Combined sources
Helixi576 – 58611Combined sources
Beta strandi589 – 5924Combined sources
Helixi597 – 5993Combined sources
Helixi600 – 6078Combined sources
Turni608 – 6103Combined sources
Beta strandi613 – 6175Combined sources
Turni619 – 6213Combined sources
Helixi623 – 6286Combined sources
Beta strandi629 – 6357Combined sources
Beta strandi646 – 6538Combined sources
Helixi656 – 6638Combined sources
Beta strandi740 – 75011Combined sources
Helixi752 – 7543Combined sources
Helixi755 – 76410Combined sources
Beta strandi768 – 7725Combined sources
Beta strandi774 – 7829Combined sources
Helixi783 – 7853Combined sources
Helixi786 – 79510Combined sources
Beta strandi799 – 8024Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 214-326, 410-669.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO29777.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 8367HMA 1PROSITE-ProRule annotationAdd
BLAST
Domaini741 – 80262HMA 2PROSITE-ProRule annotationAdd
BLAST

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

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
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. Positions 214-326, 410-669.
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.

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

BioCyciAFUL224325:GJBC-486-MONOMER.
BRENDAi3.6.3.54. 414.
SABIO-RKO29777.

Miscellaneous databases

EvolutionaryTraceiO29777.

Family and domain databases

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: April 13, 2016
This is version 123 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.