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O30085

- COPB_ARCFU

UniProt

O30085 - COPB_ARCFU

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Protein

Copper-exporting P-type ATPase B

Gene

copB

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

Functioni

Involved in copper export.2 Publications

Catalytic activityi

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

Enzyme regulationi

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

pH dependencei

Optimum pH is 5.7.2 Publications

Temperature dependencei

Optimum temperature is 85 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei389 – 38914-aspartylphosphate intermediate1 Publication
Binding sitei565 – 5651Phosphate1 Publication
Metal bindingi583 – 5831MagnesiumBy similarity
Metal bindingi587 – 5871MagnesiumBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. copper-exporting ATPase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
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-156-MONOMER.

Protein family/group databases

TCDBi3.A.3.5.10. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Copper-exporting P-type ATPase B (EC:3.6.3.4)
Gene namesi
Name:copB
Ordered Locus Names:AF_0152
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
ProteomesiUP000002199: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6464CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei65 – 8521HelicalSequence AnalysisAdd
BLAST
Topological domaini86 – 916ExtracellularSequence Analysis
Transmembranei92 – 11221HelicalSequence AnalysisAdd
BLAST
Topological domaini113 – 12715CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei128 – 14821HelicalSequence AnalysisAdd
BLAST
Topological domaini149 – 1513ExtracellularSequence Analysis
Transmembranei152 – 17221HelicalSequence AnalysisAdd
BLAST
Topological domaini173 – 303131CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei304 – 32421HelicalSequence AnalysisAdd
BLAST
Topological domaini325 – 33612ExtracellularSequence AnalysisAdd
BLAST
Transmembranei337 – 35721HelicalSequence AnalysisAdd
BLAST
Topological domaini358 – 640283CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei641 – 66121HelicalSequence AnalysisAdd
BLAST
Topological domaini662 – 6632ExtracellularSequence Analysis
Transmembranei664 – 68421HelicalSequence AnalysisAdd
BLAST
Topological domaini685 – 6906CytoplasmicSequence Analysis

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 690690Copper-exporting P-type ATPase BPRO_0000350609Add
BLAST

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi224325.AF0152.

Structurei

Secondary structure

1
690
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi376 – 3794Combined sources
Helixi380 – 3823Combined sources
Beta strandi385 – 3895Combined sources
Helixi390 – 3945Combined sources
Beta strandi395 – 40915Combined sources
Helixi411 – 42212Combined sources
Helixi428 – 43912Combined sources
Beta strandi448 – 4536Combined sources
Turni454 – 4563Combined sources
Beta strandi457 – 4626Combined sources
Beta strandi465 – 4706Combined sources
Helixi472 – 4776Combined sources
Helixi486 – 4905Combined sources
Turni491 – 4933Combined sources
Beta strandi495 – 5017Combined sources
Beta strandi504 – 51512Combined sources
Helixi519 – 52810Combined sources
Beta strandi532 – 5365Combined sources
Helixi541 – 55111Combined sources
Beta strandi554 – 5574Combined sources
Helixi562 – 5643Combined sources
Helixi565 – 5739Combined sources
Beta strandi578 – 5825Combined sources
Turni584 – 5874Combined sources
Helixi588 – 5936Combined sources
Beta strandi594 – 5996Combined sources
Beta strandi604 – 6063Combined sources
Beta strandi610 – 6145Combined sources
Helixi622 – 63110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SKXX-ray1.59A372-636[»]
3SKYX-ray2.10A372-636[»]
ProteinModelPortaliO30085.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni390 – 3912Phosphate binding
Regioni537 – 5382Phosphate binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 5150His-richAdd
BLAST

Domaini

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 similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2217.
KOiK01533.
OMAiKSKTQDL.

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.
IPR027256. Cation_transp_P-typ_ATPase_IB.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
PR00120. HATPASE.
SUPFAMiSSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O30085-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHEHDSHGEA AHSNSEDMQM IHQHHEHHGH EEEHSAHHEK MKHSADHGDH
60 70 80 90 100
HRMMMEDFKK RFYVSTLLTI PILILSPAIQ TFLGFRVEFA GSLYILFLLS
110 120 130 140 150
SAVYFYGGYP FLKGIFDELR RRQPGMMTLI AVAISVAYFY SSAVVFGLKG
160 170 180 190 200
KFFFWELATL IDIMLLGHYI EMRSVLGASR ALEELVKIMP SEAHLLKDGE
210 220 230 240 250
IVEVKVENLK PGDKVLVKPG EKIPVDGIVV EGESFVNEAM LTGESKPVAK
260 270 280 290 300
KPGDTVIGGA INGEGSLVVE VEKTGKDTYL NQVIELVRQA QESKSRTQDL
310 320 330 340 350
ANRAALLLTV IALTVGSVTL AIWLAYIADF AFAIERAVTV MVITCPHALG
360 370 380 390 400
LAIPLVVAVS TSLAAKSGLL IRDRQAFERA KDLQAVIFDK TGTLTEGRFG
410 420 430 440 450
VTDIVGFNHS EDELLQIAAS LEARSEHPIA AAIVEEAEKR GFGLTEVEEF
460 470 480 490 500
RAIPGKGVEG IVNGRRYMVV SPGYIRELGI KTDESVEKLK QQGKTVVFIL
510 520 530 540 550
KNGEVSGVIA LADRIRPESR EAISKLKAIG IKCMMLTGDN RFVAKWVAEE
560 570 580 590 600
LGLDDYFAEV LPHEKAEKVK EVQQKYVTAM VGDGVNDAPA LAQADVGIAI
610 620 630 640 650
GAGTDVAVET ADIVLVRNDP RDVAAIVELS RKTYSKMKQN LLWATGYNAF
660 670 680 690
AIPLAAGVLY SAGILLSPAV GAILMSLSTV IVAINARLLR
Length:690
Mass (Da):75,383
Last modified:January 1, 1998 - v1
Checksum:iAA063EF54B4F5EA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB91079.1.
PIRiH69268.
RefSeqiNP_068991.1. NC_000917.1.
WP_010877664.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB91079; AAB91079; AF_0152.
GeneIDi1483363.
KEGGiafu:AF0152.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB91079.1 .
PIRi H69268.
RefSeqi NP_068991.1. NC_000917.1.
WP_010877664.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3SKX X-ray 1.59 A 372-636 [» ]
3SKY X-ray 2.10 A 372-636 [» ]
ProteinModelPortali O30085.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224325.AF0152.

Protein family/group databases

TCDBi 3.A.3.5.10. the p-type atpase (p-atpase) superfamily.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB91079 ; AAB91079 ; AF_0152 .
GeneIDi 1483363.
KEGGi afu:AF0152.

Phylogenomic databases

eggNOGi COG2217.
KOi K01533.
OMAi KSKTQDL.

Enzyme and pathway databases

BioCyci AFUL224325:GJBC-156-MONOMER.

Family and domain databases

Gene3Di 2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProi IPR023299. 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 ]
Pfami PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view ]
PRINTSi PR00119. CATATPASE.
PR00120. HATPASE.
SUPFAMi SSF56784. SSF56784. 2 hits.
TIGRFAMsi TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [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.

Entry informationi

Entry nameiCOPB_ARCFU
AccessioniPrimary (citable) accession number: O30085
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 101 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

External Data

Dasty 3