ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P05425

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name COPB_ENTHR
Primary accession number P05425
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on October 1, 1993 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 70)
Name and origin of the protein
Protein name Copper-exporting P-type ATPase B
Synonym EC 3.6.3.n1
Gene name
Name: copB
From
Enterococcus hirae [TaxID: 1354] 
Taxonomy Bacteria; Firmicutes; Lactobacillales; Enterococcaceae; Enterococcus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN COPPER HOMEOSTASIS.
STRAIN=ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459;
PubMed=8048974 [NCBI, ExPASy, EBI, Israel, Japan]
Odermatt A., Suter H., Krapf R., Solioz M.;
"Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae.";
J. Biol. Chem. 268:12775-12779(1993).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 162-745.
PubMed=2953719 [NCBI, ExPASy, EBI, Israel, Japan]
Solioz M., Mathews S., Fuerst P.;
"Cloning of the K+-ATPase of Streptococcus faecalis. Structural and evolutionary implications of its homology to the KdpB-protein of Escherichia coli.";
J. Biol. Chem. 262:7358-7362(1987).
[3]
 FUNCTION IN COPPER AND SILVER EXPORT, AND INDUCTION BY COPPER AND SILVER.
STRAIN=ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459;
DOI=10.1006/bbrc.1994.1891; PubMed=8037745 [NCBI, ExPASy, EBI, Israel, Japan]
Odermatt A., Krapf R., Solioz M.;
"Induction of the putative copper ATPases, CopA and CopB, of Enterococcus hirae by Ag+ and Cu2+, and Ag+ extrusion by CopB.";
Biochem. Biophys. Res. Commun. 202:44-48(1994).
[4]
 FUNCTION IN COPPER AND SILVER EXPORT, INHIBITION BY VANADATE, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459;
PubMed=7721839 [NCBI, ExPASy, EBI, Israel, Japan]
Solioz M., Odermatt A.;
"Copper and silver transport by CopB-ATPase in membrane vesicles of Enterococcus hirae.";
J. Biol. Chem. 270:9217-9221(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L13292; AAA61836.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B45995; B45995.
3D structure databases
ModBase P05425.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005507; Molecular function: copper ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006825; Biological process: copper ion transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006416; ATPase-IB_hvy.
IPR001757; ATPase_P.
IPR006403; ATPase_P_cat/Cu.
IPR005834; Dehalogen-like_hydro.
IPR008250; E1-E2_ATPase_reg.
IPR000695; H_ATPase.
Graphical view of domain structure.
PANTHER PTHR11939; ATPase_P; 1.
Pfam PF00122; E1-E2_ATPase; 1.
PF00702; Hydrolase; 1.
Pfam graphical view of domain structure.
PRINTS PR00119; CATATPASE.
PR00120; HATPASE.
TIGRFAMs TIGR01511; ATPase-IB1_Cu; 1.
TIGR01525; ATPase-IB_hvy; 1.
TIGR01494; ATPase_P-type; 2.
PROSITE PS00154; ATPASE_E1_E2; 1.
BLOCKS P05425.
ProtoNet P05425.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cell membrane; Copper; Copper transport; Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Repeat; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   745  745     Copper-exporting P-type ATPase B. PRO_0000046251
TOPO_DOM   1   108  108     Cytoplasmic (Potential). 
TRANSMEM   109   128  20     Potential. 
TOPO_DOM   129   139  11     Extracellular (Potential). 
TRANSMEM   140   160  21     Potential. 
TOPO_DOM   161   170  10     Cytoplasmic (Potential). 
TRANSMEM   171   191  21     Potential. 
TOPO_DOM   192   200  9     Extracellular (Potential). 
TRANSMEM   201   217  17     Potential. 
TOPO_DOM   218   359  142     Cytoplasmic (Potential). 
TRANSMEM   360   379  20     Potential. 
TOPO_DOM   380   388  9     Extracellular (Potential). 
TRANSMEM   389   409  21     Potential. 
TOPO_DOM   410   703  294     Cytoplasmic (Potential). 
TRANSMEM   704   721  18     Potential. 
TOPO_DOM   722   723  2     Extracellular (Potential). 
TRANSMEM   724   744  21     Potential. 
TOPO_DOM   745   745  1     Cytoplasmic (Potential). 
REPEAT   60    71  12     1. 
REPEAT   73    84  12     2. 
REPEAT   86    97  12     3. 
REGION   60    97  38     3 X 12 AA approximate repeats. 
ACT_SITE   440   440        4-aspartylphosphate intermediate (By similarity). 
METAL   638   638        Magnesium (By similarity). 
METAL   642   642        Magnesium (By similarity). 
CONFLICT   196   196        N -> S (in Ref. 2). 
CONFLICT   329   333        NGYLA -> MVTC (in Ref. 2). 
Sequence information
Length: 745 AA [This is the length of the unprocessed precursor] Molecular weight: 81523 Da [This is the MW of the unprocessed precursor] CRC64: 956EDF22D23C8D94 [This is a checksum on the sequence] 
        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
P05425 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!