Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P05425 (COPB_ENTHR)

Last modified June 16, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Copper-exporting P-type ATPase B
    EC=3.6.3.n1
Gene names
Name: copB
OrganismEnterococcus hirae
Taxonomic identifier1354 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

Hide | Top

Protein attributes

Sequence length745 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Involved in copper export. Can also export silver. Ref.1 Ref.3 Ref.4

Catalytic activity

ATP + H2O + Cu1+(In) = ADP + phosphate + Cu1+(Out).

Enzyme regulation

Inhibited by vanadate.

Subunit structure

Monomer.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Induction

By copper and silver. Ref.3

Sequence similarities

Belongs to the cation transport ATPase (P-type) family. Type IB subfamily.

biophysicochemical properties

pH dependence:

Optimum pH is 6.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 745745Copper-exporting P-type ATPase B
PRO_0000046251

Regions

Topological domain1 – 108108Cytoplasmic Potential
Transmembrane109 – 12820 Potential
Topological domain129 – 13911Extracellular Potential
Transmembrane140 – 16021 Potential
Topological domain161 – 17010Cytoplasmic Potential
Transmembrane171 – 19121 Potential
Topological domain192 – 2009Extracellular Potential
Transmembrane201 – 21717 Potential
Topological domain218 – 359142Cytoplasmic Potential
Transmembrane360 – 37920 Potential
Topological domain380 – 3889Extracellular Potential
Transmembrane389 – 40921 Potential
Topological domain410 – 703294Cytoplasmic Potential
Transmembrane704 – 72118 Potential
Topological domain722 – 7232Extracellular Potential
Transmembrane724 – 74421 Potential
Topological domain7451Cytoplasmic Potential
Repeat60 – 71121
Repeat73 – 84122
Repeat86 – 97123
Region60 – 97383 X 12 AA approximate repeats

Sites

Active site44014-aspartylphosphate intermediate By similarity
Metal binding6381Magnesium By similarity
Metal binding6421Magnesium By similarity

Experimental info

Sequence conflict1961N → S Ref.2
Sequence conflict329 – 3335NGYLA → MVTC Ref.2

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P05425-1 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: 956EDF22D23C8D94

FASTA74581,523
        10         20         30         40         50         60 
MNNGIDPENE TNKKGAIGKN PEEKITVEQT NTKNNLQEHG KMENMDQHHT HGHMERHQQM 

        70         80         90        100        110        120 
DHGHMSGMDH SHMDHEDMSG MNHSHMGHEN MSGMDHSMHM GNFKQKFWLS LILAIPIILF 

       130        140        150        160        170        180 
SPMMGMSFPF QVTFPGSNWV VLVLATILFI YGGQPFLSGA KMELKQKSPA MMTLIAMGIT 

       190        200        210        220        230        240 
VAYVYSVYSF IANLINPHTH VMDFFWELAT LIVIMLLGHW IEMNAVSNAS DALQKLAELL 

       250        260        270        280        290        300 
PESVKRLKKD GTEETVSLKE VHEGDRLIVR AGDKMPTDGT IDKGHTIVDE SAVTGESKGV 

       310        320        330        340        350        360 
KKQVGDSVIG GSINGDGTIE ITVTGTGENG YLAKVMEMVR KAQGEKSKLE FLSDKVAKWL 

       370        380        390        400        410        420 
FYVALVVGII AFIAWLFLAN LPDALERMVT VFIIACPHAL GLAIPLVVAR STSIAAKNGL 

       430        440        450        460        470        480 
LLKNRNAMEQ ANDLDVIMLD KTGTLTQGKF TVTGIEILDE AYQEEEILKY IGALEAHANH 

       490        500        510        520        530        540 
PLAIGIMNYL KEKKITPYQA QEQKNLAGVG LEATVEDKDV KIINEKEAKR LGLKIDPERL 

       550        560        570        580        590        600 
KNYEAQGNTV SFLVVSDKLV AVIALGDVIK PEAKEFIQAI KEKNIIPVML TGDNPKAAQA 

       610        620        630        640        650        660 
VAEYLGINEY YGGLLPDDKE AIVQRYLDQG KKVIMVGDGI NDAPSLARAT IGMAIGAGTD 

       670        680        690        700        710        720 
IAIDSADVVL TNSDPKDILH FLELAKETRR KMIQNLWWGA GYNIIAIPLA AGILAPIGLI 

       730        740 
LSPAVGAVLM SLSTVVVALN ALTLK

« Hide

Hide | Top

References

[1]"Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae."
Odermatt A., Suter H., Krapf R., Solioz M.
J. Biol. Chem. 268:12775-12779(1993) [PubMed: 8048974] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN COPPER HOMEOSTASIS.
Strain: ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459.
[2]"Cloning of the K+-ATPase of Streptococcus faecalis. Structural and evolutionary implications of its homology to the KdpB-protein of Escherichia coli."
Solioz M., Mathews S., Fuerst P.
J. Biol. Chem. 262:7358-7362(1987) [PubMed: 2953719] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 162-745.
[3]"Induction of the putative copper ATPases, CopA and CopB, of Enterococcus hirae by Ag+ and Cu2+, and Ag+ extrusion by CopB."
Odermatt A., Krapf R., Solioz M.
Biochem. Biophys. Res. Commun. 202:44-48(1994) [PubMed: 8037745] [Abstract]
Cited for: FUNCTION IN COPPER AND SILVER EXPORT, INDUCTION BY COPPER AND SILVER.
Strain: ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459.
[4]"Copper and silver transport by CopB-ATPase in membrane vesicles of Enterococcus hirae."
Solioz M., Odermatt A.
J. Biol. Chem. 270:9217-9221(1995) [PubMed: 7721839] [Abstract]
Cited for: FUNCTION IN COPPER AND SILVER EXPORT, INHIBITION BY VANADATE, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459.

Hide | Top

Cross-references

Sequence databases

L13292 Genomic DNA. Translation: AAA61836.1.
PIRB45995.

3D structure databases

ModBaseSearch...

Protein family/group databases

TCDB3.A.3.5.2. P-type ATPase (P-ATPase) superfamily.

Enzyme and pathway databases

BRENDA3.6.3.4. 39265.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-reg.
IPR006403. ATPase_P-typ_cat/Cu-transptr.
IPR000695. ATPase_P-typ_H-transp.
IPR006416. ATPase_P-typ_heavy-metal.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_phosphor_site.
IPR005834. Dehalogen-like_hydro.
[Graphical view]
PANTHERPTHR11939. ATPase_P. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
TIGRFAMsTIGR01511. ATPase-IB1_Cu. 1 hit.
TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameCOPB_ENTHR
AccessionPrimary (citable) accession number: P05425
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1993
Last modified: June 16, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents