Reviewed, UniProtKB/Swiss-Prot Q8XD24 (COPA_ECO57)

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:	Z0604, ECs0537

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	834 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Involved in copper export By similarity.
Catalytic activity	ATP + H2O + Cu1+(In) = ADP + phosphate + Cu1+(Out).
Subcellular location	Cell membrane; Multi-pass membrane protein Probable.
Sequence similarities	Belongs to the cation transport ATPase (P-type) family. Type IB subfamily. Contains 2 HMA domains.

Ontologies

Keywords
Biological process	Copper transport Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Repeat 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: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 834	833	Copper-exporting P-type ATPase A		PRO_0000046321
Regions
	Transmembrane	187 – 207	21	Potential
	Transmembrane	218 – 238	21	Potential
	Transmembrane	254 – 274	21	Potential
	Transmembrane	284 – 304	21	Potential
	Transmembrane	438 – 458	21	Potential
	Transmembrane	464 – 484	21	Potential
	Transmembrane	779 – 799	21	Potential
	Transmembrane	801 – 821	21	Potential
	Domain	4 – 65	62	HMA 1
	Domain	100 – 163	64	HMA 2
Sites
	Active site	523	1	4-aspartylphosphate intermediate Probable
	Metal binding	14	1	Copper Potential
	Metal binding	17	1	Copper Potential
	Metal binding	110	1	Copper Potential
	Metal binding	113	1	Copper Potential
	Metal binding	720	1	Magnesium By similarity
	Metal binding	724	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8XD24-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: B4789F2CCF12E9FB	FASTA	834	88,005
	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

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." 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. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." 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. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005174 Genomic DNA. Translation: AAG54833.1. BA000007 Genomic DNA. Translation: BAB33960.1.
PIR	A90696. E85546.
RefSeq	NP_286225.1. NP_308564.1.
3D structure databases
HSSP	HSSP built from PDB template 1AFJ based on UniProtKB P04129.
ModBase	Search...
Genome annotation databases
GeneID	914641. 957460.
GenomeReviews	Gene locus Z0604 in contig AE005174_GR. Gene locus ECs0537 in contig BA000007_GR.
KEGG	ece:Z0604. ecs:ECs0537.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8XD24.
OMA	Q8XD24. SCVSRVQ.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS0537-MON.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-reg. IPR006403. ATPase_P-typ_cat/Cu-transptr. IPR000695. ATPase_P-typ_H-transp. 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. 2 hits. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00120. HATPASE.
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. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COPA_ECO57

Accession

Primary (citable) accession number: Q8XD24

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2002
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 61 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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