Copper-transporting ATPase - Helicobacter pylori J99

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Reviewed, UniProtKB/Swiss-Prot Q9ZM69 (COPA_HELPJ)

Last modified June 16, 2009. Version 71. History...

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

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Names and origin

Protein names

Recommended name:
Copper-transporting ATPase
EC=3.6.3.4

Gene names

Name:	copA
Ordered Locus Names:	jhp_0353

Organism

Helicobacter pylori J99 (Campylobacter pylori J99) [Complete proteome] [HAMAP]

Taxonomic identifier

85963 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

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Protein attributes

Sequence length	745 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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General annotation (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.
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IB subfamily. Contains 1 HMA domain.

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Ontologies

Keywords
Biological process	Copper transport Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Ligand	ATP-binding Copper Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro copper ion transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW copper-exporting ATPase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 745

745

Copper-transporting ATPase

PRO_0000046174

Regions

Topological domain

1 – 83

Cytoplasmic Potential

Transmembrane

84 – 104

Potential

Topological domain

105 – 124

Extracellular Potential

Transmembrane

125 – 144

Potential

Topological domain

145 – 151

Cytoplasmic Potential

Transmembrane

152 – 172

Potential

Topological domain

173 – 194

Extracellular Potential

Transmembrane

195 – 215

Potential

Topological domain

216 – 343

128

Cytoplasmic Potential

Transmembrane

344 – 366

Potential

Topological domain

367 – 379

Extracellular Potential

Transmembrane

380 – 397

Potential

Topological domain

398 – 685

288

Cytoplasmic Potential

Transmembrane

686 – 705

Potential

Topological domain

706 – 716

Extracellular Potential

Transmembrane

717 – 735

Potential

Topological domain

736 – 745

Cytoplasmic Potential

Domain

2 – 68

HMA

Sites

Active site

435

4-aspartylphosphate intermediate By similarity

Metal binding

Copper Potential

Metal binding

Copper Potential

Metal binding

631

Magnesium By similarity

Metal binding

635

Magnesium By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9ZM69-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 69E5CD155579C59F
Show »

FASTA

745

81,912

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

        70         80         90        100        110        120 
KLGYSPKKTL AEEKKEFFSP NVKLALAVIF TLFVVYLSMG AMLSPSLLPE SLLTINHHSN 

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

       190        200        210        220        230        240 
NHYTDQWSYG HYYFESVCVI LMFVMVGKRI ENVSKDKALD AMQALMKNAP KTALKMHNNQ 

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

       310        320        330        340        350        360 
LNSNTSFLMK ATQDNKNSTL SQIIEMIHNA QSSKAEISRL ADKVSSVFVP SVIAIAVLAF 

       370        380        390        400        410        420 
VVWLIIAPKP DFWWNFRTAL EVFVSVLVIS CPCALGLATP MSILVANQKA SSLGLFFKDA 

       430        440        450        460        470        480 
KSLEKARLVN TIVFDKTGTL TNGKPVVKSI HSNIELLELL SLASSIEKSS EHVIAKGIVE 

       490        500        510        520        530        540 
YAKERNAPLK DISEVKVKTG FGISAKVDYQ GAKEIIKVGN SEFFNPINTL EIKENGILVF 

       550        560        570        580        590        600 
VGRAINEKED ELLGAFVLED LPKKGVKEHI 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

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References

[1]

"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.

Trust T.J.
Nature 397:176-180(1999) [PubMed: 9923682] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases
	AE001439 Genomic DNA. Translation: AAD05935.1.
PIR	A71941.
RefSeq	NP_223072.1.
3D structure databases
HSSP	HSSP built from PDB template 1CPZ based on UniProtKB Q47840.
ModBase	Search...
Genome annotation databases
GeneID	889106.
GenomeReviews	Gene locus jhp_0353 in contig AE001439_GR.
KEGG	hpj:jhp0353.
NMPDR	fig\|85963.1.peg.350.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9ZM69.
OMA	Q9ZM69. VCAGRIE.
Enzyme and pathway databases
BioCyc	HPYL85963:JHP0353-MON.
BRENDA	3.6.3.4. 295085.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-reg. IPR006403. ATPase_P-typ_cat/Cu-transptr. IPR001756. ATPase_P-typ_Cu-transptr. IPR006416. ATPase_P-typ_heavy-metal. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_phosphor_site. IPR005834. Dehalogen-like_hydro. IPR017969. Heavy-metal-associated_CS. IPR006121. HeavyMe_transpt. [Graphical view]
PANTHER	PTHR11939. ATPase_P. 1 hit.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00403. HMA. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00943. CUATPASE.
TIGRFAMs	TIGR01511. ATPase-IB1_Cu. 1 hit. TIGR01525. ATPase-IB_hvy. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. PS01047. HMA_1. 1 hit. PS50846. HMA_2. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

COPA_HELPJ

Accession

Primary (citable) accession number: Q9ZM69

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents