Copper-exporting P-type ATPase A - Staphylococcus aureus (strain USA300 / TCH1516)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Copper-exporting P-type ATPase A
EC=3.6.3.n1

Gene names

Name:	copA
Ordered Locus Names:	USA300HOU_2552

Organism

Staphylococcus aureus (strain USA300 / TCH1516) [Complete proteome] [HAMAP]

Taxonomic identifier

451516 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

Protein attributes

Sequence length	802 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in copper export By similarity.
Catalytic activity	ATP + H₂O + Cu⁺(In) = ADP + phosphate + Cu⁺(Out).
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification] Contains 2 HMA domains.

Ontologies

Keywords
Biological process	Copper transport Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Copper Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
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: InterPro copper-transporting ATPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 802

802

Copper-exporting P-type ATPase A

PRO_0000350595

Regions

Transmembrane

161 – 181

21

Helical; Potential

Transmembrane

192 – 212

21

Helical; Potential

Transmembrane

224 – 244

21

Helical; Potential

Transmembrane

256 – 276

21

Helical; Potential

Transmembrane

411 – 431

21

Helical; Potential

Transmembrane

438 – 458

21

Helical; Potential

Transmembrane

748 – 767

20

Helical; Potential

Transmembrane

771 – 790

20

Helical; Potential

Domain

6 – 71

66

HMA 1

Domain

73 – 139

67

HMA 2

Sites

Active site

495

1

4-aspartylphosphate intermediate By similarity

Metal binding

16

1

Copper 1 By similarity

Metal binding

19

1

Copper 1 By similarity

Metal binding

83

1

Copper 2 By similarity

Metal binding

86

1

Copper 2 By similarity

Metal binding

690

1

Magnesium By similarity

Metal binding

694

1

Magnesium By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A8Z3F8 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: A56904C94A137010
Show »

FASTA

802

86,770

        10         20         30         40         50         60 
MANTKKTTLD ITGMTCAACS NRIEKKLNKL DDVNAQVNLT TEKATVEYNP DQHDVQEFIN 

        70         80         90        100        110        120 
TIQHLGYGVA VETVELDITG MTCAACSSRI EKVLNKMDGV QNATVNLTTE QAKVDYYPEE 

       130        140        150        160        170        180 
TDADKLVTRI QKLGYDASIK DNNKDQTSRK AEALQHKLIK LIISAVLSLP LLMLMFVHLF 

       190        200        210        220        230        240 
NMHIPALFTN PWFQFILATP VQFIIGWQFY VGAYKNLRNG GANMDVLVAV GTSAAYFYSI 

       250        260        270        280        290        300 
YEMVRWLNGS TTQPHLYFET SAVLITLILF GKYLEARAKS QTTNALGELL SLQAKEARIL 

       310        320        330        340        350        360 
KDGNEVMIPL NEVHVGDTLI VKPGEKIPVD GKIIKGMTAI DESMLTGESI PVEKNVDDTV 

       370        380        390        400        410        420 
IGSTMNKNGT ITMTATKVGG DTALANIIKV VEEAQSSKAP IQRLADIISG YFVPIVVGIA 

       430        440        450        460        470        480 
LLTFIVWITL VTPGTFEPAL VASISVLVIA CPCALGLATP TSIMVGTGRA AENGILFKGG 

       490        500        510        520        530        540 
EFVERTHQID TIVLDKTGTI TNGRPVVTDY HGDNQTLQLL ATAEKDSEHP LAEAIVNYAK 

       550        560        570        580        590        600 
EKQLILTETT TFKAVPGHGI EATIDHHYIL VGNRKLMADN DISLPKHISD DLTHYERDGK 

       610        620        630        640        650        660 
TAMLIAVNYS LTGIIAVADT VKDHAKDAIK QLHDMGIEVA MLTGDNKNTA QAIAKQVGID 

       670        680        690        700        710        720 
TVIADILPEE KAAQIAKLQQ QGKKVAMVGD GVNDAPALVK ADIGIAIGTG TEVAIEAADI 

       730        740        750        760        770        780 
TILGGDLMLI PKAIYASKAT IRNIRQNLFW AFGYNIAGIP IAALGLLAPW VAGAAMALSS 

       790        800 
VSVVTNALRL KKMRLEPRRK DA

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References

[1]

"Subtle genetic changes enhance virulence of methicillin resistant and sensitive Staphylococcus aureus."
Highlander S.K., Hulten K.G., Qin X., Jiang H., Yerrapragada S., Mason E.O. Jr., Shang Y., Williams T.M., Fortunov R.M., Liu Y., Igboeli O., Petrosino J., Tirumalai M., Uzman A., Fox G.E., Cardenas A.M., Muzny D.M., Hemphill L.

Weinstock G.M.
BMC Microbiol. 7:99-99(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: USA300 / TCH1516.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000730 Genomic DNA. Translation: ABX30538.1.
RefSeq	YP_001576417.1. NC_010079.1.
3D structure databases
ProteinModelPortal	A8Z3F8.
ModBase	Search...
Protein-protein interaction databases
STRING	451516.USA300HOU_2552.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABX30538; ABX30538; USA300HOU_2552.
GeneID	5774842.
KEGG	sax:USA300HOU_2552.
PATRIC	19600392. VBIStaAur36919_2664.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2217.
HOGENOM	HOG000250397.
KO	K01533.
OMA	EQDGSTD.
ProtClustDB	CLSK886068.
Enzyme and pathway databases
BioCyc	SAUR451516:GJQ4-2641-MONOMER.
Family and domain databases
Gene3D	2.70.150.10. 1 hit. 3.40.1110.10. 1 hit. 3.40.50.1000. 2 hits.
InterPro	IPR023299. ATPase_P-typ_cyto_domN. IPR018303. ATPase_P-typ_P_site. IPR008250. ATPase_P-typ_transduc_dom_A. IPR027256. Cation_transp_P-typ_ATPase_IB. IPR001757. Cation_transp_P_typ_ATPase. IPR027183. Cu-transptr_ATPase. IPR023214. HAD-like_dom. IPR017969. Heavy-metal-associated_CS. IPR006121. HeavyMe-assoc_HMA. IPR006122. HMA_Cu_ion-bd. [Graphical view]
PANTHER	PTHR24093. PTHR24093. 1 hit. PTHR24093:SF50. PTHR24093:SF50. 1 hit.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00403. HMA. 2 hits. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE.
SUPFAM	SSF56784. HAD-like_dom. 1 hit. SSF55008. HeavyMe_transpt. 2 hits.
TIGRFAMs	TIGR01525. ATPase-IB_hvy. 1 hit. TIGR01494. ATPase_P-type. 1 hit. TIGR00003. TIGR00003. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. PS01047. HMA_1. 2 hits. PS50846. HMA_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COPA_STAAT

Accession

Primary (citable) accession number: A8Z3F8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	January 15, 2008
Last modified:	May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

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

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents