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 Q8XD24


[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 ATCU_ECO57
Primary accession number Q8XD24
Secondary accession numbers None
Integrated into Swiss-Prot on April 3, 2002
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 53)
Name and origin of the protein
Protein name Copper-transporting P-type ATPase
Synonym EC 3.6.3.4
Gene name
Name: copA
OrderedLocusNames: Z0604, ECs0537
From
Escherichia coli O157:H7 [TaxID: 83334] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
DOI=10.1038/35054089; PubMed=11206551 [NCBI, ExPASy, EBI, Israel, Japan]
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.;
"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
Nature 409:529-533(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
DOI=10.1093/dnares/8.1.11; PubMed=11258796 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., Shiba T., Hattori M., Shinagawa H.;
"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12.";
DNA Res. 8:11-22(2001).
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
AE005174; AAG54833.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000007; BAB33960.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A90696; A90696.
E85546; E85546.
RefSeq NP_286225.1; -.
NP_308564.1; -.
3D structure databases
HSSP P04129; 1AFJ. [HSSP ENTRY / PDB]
ModBase Q8XD24.
Enzyme and pathway databases
BioCyc ECOL83334:ECS0537-MON; -.
Ontologies
GO
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
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.
IPR006121; HeavyMe_transpt.
Graphical view of domain structure.
PANTHER PTHR11939; ATPase_P; 1.
Pfam PF00122; E1-E2_ATPase; 1.
PF00403; HMA; 2.
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.
PS01047; HMA_1; 1.
PS50846; HMA_2; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q8XD24.
Genome annotation databases
GeneID 914641; -.
957460; -.
GenomeReviews BA000007_GR; ECs0537.
AE005174_GR; Z0604.
KEGG ece:Z0604; -.
ecs:ECs0537; -.
Phylogenomic databases
HOGENOM Q8XD24; -.
Genome annotation databases
CMR Q8XD24; Z0604.
Other
ProtoNet Q8XD24.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cell membrane; Complete proteome; 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
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   834  833     Copper-transporting P-type ATPase. PRO_0000046321
TRANSMEM   187   207  21     Potential. 
TRANSMEM   218   238  21     Potential. 
TRANSMEM   254   274  21     Potential. 
TRANSMEM   284   304  21     Potential. 
TRANSMEM   438   458  21     Potential. 
TRANSMEM   464   484  21     Potential. 
TRANSMEM   779   799  21     Potential. 
TRANSMEM   801   821  21     Potential. 
DOMAIN   4    65  62     HMA 1. 
DOMAIN   100   163  64     HMA 2. 
ACT_SITE   523   523        4-aspartylphosphate intermediate (Probable). 
METAL   14    14        Copper (Potential). 
METAL   17    17        Copper (Potential). 
METAL   110   110        Copper (Potential). 
METAL   113   113        Copper (Potential). 
METAL   720   720        Magnesium (By similarity). 
METAL   724   724        Magnesium (By similarity). 
Sequence information
Length: 834 AA [This is the length of the unprocessed precursor] Molecular weight: 88005 Da [This is the MW of the unprocessed precursor] CRC64: B4789F2CCF12E9FB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSQTIDLTLD GLSCGHCVKR VKESLEQRPD VEQADVSITE AHVTGTASAE QLIETIKQAG 

        70         80         90        100        110        120 
YDASVSHPKA KPLAESSIPS EALTAVSEAL PAATADDDDS QQLLLSGMSC ASCVTRVQNA 

       130        140        150        160        170        180 
LQSVPGVTQA RVNLAERTAL VMGSASPQDL VQAVEKAGYG AEAIEDDAKR RERQQETAVA 

       190        200        210        220        230        240 
TMKRFRWQAI VALAVGIPVM VWGMIGDNMM VTADNRSLWL VIGLITLAVM VFAGGHFYRS 

       250        260        270        280        290        300 
AWKSLLNGAA TMDTLVALGT GVAWLYSMSV NLWPQWFPME ARHLYYEASA MIIGLINLGH 

       310        320        330        340        350        360 
MLEARARQRS SKALEKLLDL TPPTARLVTD EGEKSVPLAE VQPGMLLRLT TGDRVPVDGE 

       370        380        390        400        410        420 
ITQGEAWLDE AMLTGEPIPQ QKGEGDSVHA GTVVQDGSVL FRASAVGSHT TLSRIIRMVR 

       430        440        450        460        470        480 
QAQSSKPEIG QLADKISAVF VPVVVVIALV SAAIWYFFGP APQIVYTLVI ATTVLIIACP 

       490        500        510        520        530        540 
CALGLATPMS IISGVGRAAE FGVLVRDADA LQRASTLDTV VFDKTGTLTE GKPQVVAVKT 

       550        560        570        580        590        600 
FADFDEAQAL RLAAALEQGS SHPLARAILD KASDMQLPQV NGFRTLRGLG VSGEAEGHAL 

       610        620        630        640        650        660 
LLGNQALLND QQVDTKAIEA DISAQASQGA TPVLLAVDGK AVALLAVRDP LRSDSVAALQ 

       670        680        690        700        710        720 
RLHKAGYRLV MLTGDNPTTA NAIAKEAGID EVIAGVLPDG KAEAIKRLQS EGRQVAMVGD 

       730        740        750        760        770        780 
GINDAPALAQ ADVGIAMGGG SDVAIETAAI TLMRHSLMGV ADALAISRAT LRNMKQNLLG 

       790        800        810        820        830 
AFIYNSIGIP VAAGILWPFT GTLLNPVVAG AAMALSSITV VSNANRLLRF KPKE 

Q8XD24 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!