[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 43629 / JCM 7656 / NCTC 11639 / UA802; PubMed=7752900 [NCBI, ExPASy, EBI, Israel, Japan] Ge Z., Hiratsuka K., Taylor D.E.; "Nucleotide sequence and mutational analysis indicate that two Helicobacter pylori genes encode a P-type ATPase and a cation-binding protein associated with copper transport."; Mol. Microbiol. 15:97-106(1995).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 43629 / JCM 7656 / NCTC 11639 / UA802; DOI=10.1016/S0378-1097(96)00405-3; PubMed=8961555 [NCBI, ExPASy, EBI, Israel, Japan] Ge Z., Taylor D.E.; "Helicobacter pylori genes hpcopA and hpcopP constitute a cop operon involved in copper export."; FEMS Microbiol. Lett. 145:181-188(1996).

Comments

FUNCTION: Probably involved in copper export.
CATALYTIC ACTIVITY: ATP + H₂O + Cu²⁺(In) = ADP + phosphate + Cu²⁺(Out).
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
SIMILARITY: Belongs to the cation transport ATPase (P-type) family. Type IB subfamily.
SIMILARITY: Contains 1 HMA domain.
SEQUENCE CAUTION:
- Sequence=AAB67320.1; Type=Frameshift; Positions=393, 400, 410, 416, 537, 539;

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

L33259; AAB67320.1; ALT_FRAME; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q47840; 1CPZ. [HSSP ENTRY / PDB]

ModBase

P77871.

Family and domain databases

InterPro

IPR006416; ATPase-IB_hvy.
IPR001757; ATPase_P.
IPR006403; ATPase_P_cat/Cu.
IPR001756; ATPase_P_Cu.
IPR005834; Dehalogen-like_hydro.
IPR008250; E1-E2_ATPase_reg.
IPR006121; HeavyMe_transpt.
Graphical view of domain structure.

PANTHER

PTHR11939; ATPase_P; 1.

Pfam

PF00122; E1-E2_ATPase; 1.
PF00403; HMA; 1.
PF00702; Hydrolase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00119; CATATPASE.
PR00943; CUATPASE.

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; 1.
PROSITE graphical view of domain structure (profiles).

Other

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; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 745`	`745`	`Copper-transporting ATPase.`	`PRO_0000046171`
`TOPO_DOM`	`1 83`	`83`	`Cytoplasmic (Potential).`
`TRANSMEM`	`84 104`	`21`	`Potential.`
`TOPO_DOM`	`105 124`	`20`	`Extracellular (Potential).`
`TRANSMEM`	`125 144`	`20`	`Potential.`
`TOPO_DOM`	`145 151`	`7`	`Cytoplasmic (Potential).`
`TRANSMEM`	`152 172`	`21`	`Potential.`
`TOPO_DOM`	`173 194`	`22`	`Extracellular (Potential).`
`TRANSMEM`	`195 215`	`21`	`Potential.`
`TOPO_DOM`	`216 343`	`128`	`Cytoplasmic (Potential).`
`TRANSMEM`	`344 366`	`23`	`Potential.`
`TOPO_DOM`	`367 379`	`13`	`Extracellular (Potential).`
`TRANSMEM`	`380 397`	`18`	`Potential.`
`TOPO_DOM`	`398 685`	`288`	`Cytoplasmic (Potential).`
`TRANSMEM`	`686 705`	`20`	`Potential.`
`TOPO_DOM`	`706 716`	`11`	`Extracellular (Potential).`
`TRANSMEM`	`717 735`	`19`	`Potential.`
`TOPO_DOM`	`736 745`	`10`	`Cytoplasmic (Potential).`
`DOMAIN`	`2 68`	`67`	`HMA.`
`ACT_SITE`	`435 435`		`4-aspartylphosphate intermediate (By similarity).`
`METAL`	`12 12`		`Copper (Potential).`
`METAL`	`15 15`		`Copper (Potential).`
`METAL`	`631 631`		`Magnesium (By similarity).`
`METAL`	`635 635`		`Magnesium (By similarity).`

Sequence information

Length: 745 AA [This is the length of the unprocessed precursor]

Molecular weight: 82029 Da [This is the MW of the unprocessed precursor]

CRC64: 043168CF0622245B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKESFYIEGM TCTACSSGIE RSLGRKSFVK KIEVNLLNKS ANIEFNENET NLDEIFKLIE 

        70         80         90        100        110        120 
KLGYSPKKTL AEEKKEFFSP NVKLALAVIF TLFVVYLSMG AMLSPSLLPK SLLAIDNHSN 

       130        140        150        160        170        180 
FLNACLQLIG TLIVMHWGRD FYIQGFKALW HRQPNMSSLI AIGTSAALIS SLWQLYLVYT 

       190        200        210        220        230        240 
DHYTDQWSYG HYYFESVCVI LMFVMVGKRI ENVSKDKALD AMQALMKNAP KTALKIQNDQ 

       250        260        270        280        290        300 
QIEVLVDSIV VGDILKVLPG TLIAVDGEII EGEGELDESM LSGEALPVYK KVGDKVFSGT 

       310        320        330        340        350        360 
FNSHTSFLMK ATQNNKNSTL SQIVEMIHNA QSSKAEISRL ADKVSSVFVP SVIAIAILAF 

       370        380        390        400        410        420 
VVWLIIAPKP DFWWNFGIAL EVFVSVLVIS CPCALGLATL MSILVANQKA SSLGLFFKDA 

       430        440        450        460        470        480 
KSLEKARLVN TIVFDKTGTL TNGKPVVKSV HSKIELLELL SLANSIEKSS EHVIAKGIVE 

       490        500        510        520        530        540 
YAKEHNAPLK EMSEVKVKTG FGISAKTDYQ GTKEIIKVGN SEFFNPINTL EIQENGILVL 

       550        560        570        580        590        600 
VGRAINEKED ELLGAFVLED LPKKGVKEHV AQIKNLGINT FLLSGDNREN VKKCALELGI 

       610        620        630        640        650        660 
DGYISNAKPQ DKLNKIKELK EKGRIVMMVG DGLNDAPSLA MSDVAVVMAK GSDVSVQAAD 

       670        680        690        700        710        720 
IVSFNNDIKS VYSAIKLSQA TIKNIKENLF WAFCYNSVFI PLACGVLYKA NIMLSPAIAG 

       730        740 
LAMSLSSVSV VLNSQRLRNF KIKDH

P77871 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools