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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: 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)DescriptionActionsGraphical viewLength
Active sitei3894-aspartylphosphate intermediate1 Publication1
Binding sitei565Phosphate1 Publication1
Metal bindingi583MagnesiumBy similarity1
Metal bindingi587MagnesiumBy similarity1

GO - Molecular functioni

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

BRENDAi3.6.3.4. 414.

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
Proteomesi
  • UP000002199 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 64CytoplasmicSequence analysisAdd BLAST64
Transmembranei65 – 85HelicalSequence analysisAdd BLAST21
Topological domaini86 – 91ExtracellularSequence analysis6
Transmembranei92 – 112HelicalSequence analysisAdd BLAST21
Topological domaini113 – 127CytoplasmicSequence analysisAdd BLAST15
Transmembranei128 – 148HelicalSequence analysisAdd BLAST21
Topological domaini149 – 151ExtracellularSequence analysis3
Transmembranei152 – 172HelicalSequence analysisAdd BLAST21
Topological domaini173 – 303CytoplasmicSequence analysisAdd BLAST131
Transmembranei304 – 324HelicalSequence analysisAdd BLAST21
Topological domaini325 – 336ExtracellularSequence analysisAdd BLAST12
Transmembranei337 – 357HelicalSequence analysisAdd BLAST21
Topological domaini358 – 640CytoplasmicSequence analysisAdd BLAST283
Transmembranei641 – 661HelicalSequence analysisAdd BLAST21
Topological domaini662 – 663ExtracellularSequence analysis2
Transmembranei664 – 684HelicalSequence analysisAdd BLAST21
Topological domaini685 – 690CytoplasmicSequence analysis6

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003506091 – 690Copper-exporting P-type ATPase BAdd BLAST690

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi224325.AF0152.

Structurei

Secondary structure

1690
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi376 – 379Combined sources4
Helixi380 – 382Combined sources3
Beta strandi385 – 389Combined sources5
Helixi390 – 394Combined sources5
Beta strandi395 – 409Combined sources15
Helixi411 – 422Combined sources12
Helixi428 – 439Combined sources12
Beta strandi448 – 453Combined sources6
Turni454 – 456Combined sources3
Beta strandi457 – 462Combined sources6
Beta strandi465 – 470Combined sources6
Helixi472 – 477Combined sources6
Helixi486 – 490Combined sources5
Turni491 – 493Combined sources3
Beta strandi495 – 501Combined sources7
Beta strandi504 – 515Combined sources12
Helixi519 – 528Combined sources10
Beta strandi532 – 536Combined sources5
Helixi541 – 551Combined sources11
Beta strandi554 – 557Combined sources4
Helixi562 – 564Combined sources3
Helixi565 – 573Combined sources9
Beta strandi578 – 582Combined sources5
Turni584 – 587Combined sources4
Helixi588 – 593Combined sources6
Beta strandi594 – 599Combined sources6
Beta strandi604 – 606Combined sources3
Beta strandi610 – 614Combined sources5
Helixi622 – 631Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SKXX-ray1.59A372-636[»]
3SKYX-ray2.10A372-636[»]
ProteinModelPortaliO30085.
SMRiO30085.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni390 – 391Phosphate binding2
Regioni537 – 538Phosphate binding2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 51His-richAdd BLAST50

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

eggNOGiarCOG01576. Archaea.
COG2217. LUCA.
KOiK01533.
OMAiFPGSAWV.

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.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00120. 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.
RefSeqiWP_010877664.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB91079; AAB91079; AF_0152.
GeneIDi24793702.
KEGGiafu:AF_0152.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB91079.1.
PIRiH69268.
RefSeqiWP_010877664.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SKXX-ray1.59A372-636[»]
3SKYX-ray2.10A372-636[»]
ProteinModelPortaliO30085.
SMRiO30085.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF0152.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB91079; AAB91079; AF_0152.
GeneIDi24793702.
KEGGiafu:AF_0152.

Phylogenomic databases

eggNOGiarCOG01576. Archaea.
COG2217. LUCA.
KOiK01533.
OMAiFPGSAWV.

Enzyme and pathway databases

BRENDAi3.6.3.4. 414.

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.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00120. 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]
ProtoNetiSearch...

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 2, 2016
This is version 112 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.