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Protein

Copper-exporting P-type ATPase A

Gene

copA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in copper export. May also be involved in silver export.1 Publication

Catalytic activityi

ATP + H2O + Cu+(Side 1) = ADP + phosphate + Cu+(Side 2).

Enzyme regulationi

Phosphorylation is inhibited by vanadate and sensitive to KOH and hydroxylamine. Phosphorylation is Cu+-dependent.1 Publication

Kineticsi

  1. KM=1.5 µM for copper1 Publication
  2. KM=0.5 mM for ATP1 Publication
  1. Vmax=0.19 µmol/min/mg enzyme (in the presence of Cu+)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi14 – 141CopperPROSITE-ProRule annotation
Metal bindingi17 – 171CopperPROSITE-ProRule annotation
Metal bindingi110 – 1101CopperPROSITE-ProRule annotation
Metal bindingi113 – 1131CopperPROSITE-ProRule annotation
Active sitei523 – 52314-aspartylphosphate intermediateCurated
Metal bindingi720 – 7201MagnesiumPROSITE-ProRule annotation
Metal bindingi724 – 7241MagnesiumPROSITE-ProRule annotation

GO - Molecular functioni

  • ATPase activity Source: EcoliWiki
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism Source: EcoCyc
  • ATP binding Source: UniProtKB-KW
  • copper-transporting ATPase activity Source: GO_Central
  • metal ion binding Source: UniProtKB-KW
  • silver ion transmembrane transporter activity Source: EcoCyc

GO - Biological processi

  • cellular response to copper ion Source: EcoCyc
  • cellular response to silver ion Source: EcoCyc
  • copper ion export Source: EcoCyc
  • copper ion transport Source: EcoliWiki
  • detoxification of copper ion Source: EcoliWiki
  • silver ion transmembrane transport Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Copper transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Copper, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:G6260-MONOMER.
ECOL316407:JW0473-MONOMER.
MetaCyc:G6260-MONOMER.
SABIO-RKQ59385.

Protein family/group databases

TCDBi3.A.3.5.5. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Copper-exporting P-type ATPase A (EC:3.6.3.54)
Alternative name(s):
Cu(+)-exporting ATPase
Gene namesi
Name:copA
Synonyms:ybaR
Ordered Locus Names:b0484, JW0473
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13246. copA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei187 – 20721HelicalSequence analysisAdd
BLAST
Transmembranei218 – 23821HelicalSequence analysisAdd
BLAST
Transmembranei254 – 27421HelicalSequence analysisAdd
BLAST
Transmembranei284 – 30421HelicalSequence analysisAdd
BLAST
Transmembranei438 – 45821HelicalSequence analysisAdd
BLAST
Transmembranei464 – 48421HelicalSequence analysisAdd
BLAST
Transmembranei779 – 79921HelicalSequence analysisAdd
BLAST
Transmembranei801 – 82121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • intracellular membrane-bounded organelle Source: GO_Central
  • intrinsic component of membrane Source: EcoliWiki
  • membrane Source: UniProtKB
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 150143Missing : Loss of activity. Add
BLAST
Mutagenesisi14 – 141C → A: No effect. 1 Publication
Mutagenesisi17 – 171C → A: No effect. 1 Publication
Mutagenesisi110 – 1101C → A: No effect. 1 Publication
Mutagenesisi113 – 1131C → A: No effect. 1 Publication
Mutagenesisi479 – 4791C → A: Loss of copper resistance, transport and phosphoenzyme formation. 1 Publication
Mutagenesisi481 – 4811C → A or H: Loss of copper resistance, transport and phosphoenzyme formation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 834833Copper-exporting P-type ATPase APRO_0000046320Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ59385.
PRIDEiQ59385.

Expressioni

Inductioni

Transcriptionally regulated by CueR in response to Cu+ or Ag+ ions.

Interactioni

Protein-protein interaction databases

BioGridi4261336. 9 interactions.
IntActiQ59385. 6 interactions.
STRINGi511145.b0484.

Structurei

3D structure databases

ProteinModelPortaliQ59385.
SMRiQ59385. Positions 4-164, 182-829.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 6562HMA 1PROSITE-ProRule annotationAdd
BLAST
Domaini100 – 16364HMA 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 HMA domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C59. Bacteria.
COG2217. LUCA.
HOGENOMiHOG000250397.
InParanoidiQ59385.
KOiK17686.
OMAiQDGSTDH.
PhylomeDBiQ59385.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HMA_dom.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 2 hits.
[Graphical view]
PRINTSiPR00120. HATPASE.
SUPFAMiSSF55008. SSF55008. 2 hits.
SSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q59385-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQTIDLTLD GLSCGHCVKR VKESLEQRPD VEQADVSITE AHVTGTASAE
60 70 80 90 100
QLIETIKQAG YDASVSHPKA KPLAESSIPS EALTAVSEAL PAATADDDDS
110 120 130 140 150
QQLLLSGMSC ASCVTRVQNA LQSVPGVTQA RVNLAERTAL VMGSASPQDL
160 170 180 190 200
VQAVEKAGYG AEAIEDDAKR RERQQETAVA TMKRFRWQAI VALAVGIPVM
210 220 230 240 250
VWGMIGDNMM VTADNRSLWL VIGLITLAVM VFAGGHFYRS AWKSLLNGAA
260 270 280 290 300
TMDTLVALGT GVAWLYSMSV NLWPQWFPME ARHLYYEASA MIIGLINLGH
310 320 330 340 350
MLEARARQRS SKALEKLLDL TPPTARLVTD EGEKSVPLAE VQPGMLLRLT
360 370 380 390 400
TGDRVPVDGE ITQGEAWLDE AMLTGEPIPQ QKGEGDSVHA GTVVQDGSVL
410 420 430 440 450
FRASAVGSHT TLSRIIRMVR QAQSSKPEIG QLADKISAVF VPVVVVIALV
460 470 480 490 500
SAAIWYFFGP APQIVYTLVI ATTVLIIACP CALGLATPMS IISGVGRAAE
510 520 530 540 550
FGVLVRDADA LQRASTLDTV VFDKTGTLTE GKPQVVAVKT FADVDEAQAL
560 570 580 590 600
RLAAALEQGS SHPLARAILD KAGDMQLPQV NGFRTLRGLG VSGEAEGHAL
610 620 630 640 650
LLGNQALLNE QQVGTKAIEA EITAQASQGA TPVLLAVDGK AVALLAVRDP
660 670 680 690 700
LRSDSVAALQ RLHKAGYRLV MLTGDNPTTA NAIAKEAGID EVIAGVLPDG
710 720 730 740 750
KAEAIKHLQS EGRQVAMVGD GINDAPALAQ ADVGIAMGGG SDVAIETAAI
760 770 780 790 800
TLMRHSLMGV ADALAISRAT LHNMKQNLLG AFIYNSIGIP VAAGILWPFT
810 820 830
GTLLNPVVAG AAMALSSITV VSNANRLLRF KPKE
Length:834
Mass (Da):87,873
Last modified:January 23, 2007 - v4
Checksum:iCF84A18FE208E6F6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 18120EAIED…TAVAT → KRLKMTLNAASASKKPPSLA in AAB02268 (Ref. 1) CuratedAdd
BLAST
Sequence conflicti508 – 5081A → R in AAB02268 (Ref. 1) Curated
Sequence conflicti576 – 5761Q → R in AAB02268 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58330 Genomic DNA. Translation: AAB02268.1.
U82664 Genomic DNA. Translation: AAB40238.1.
U00096 Genomic DNA. Translation: AAC73586.1.
AP009048 Genomic DNA. Translation: BAE76263.1.
PIRiC64779.
RefSeqiNP_415017.1. NC_000913.3.
WP_000083955.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73586; AAC73586; b0484.
BAE76263; BAE76263; BAE76263.
GeneIDi946106.
KEGGiecj:JW0473.
eco:b0484.
PATRICi32116127. VBIEscCol129921_0505.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58330 Genomic DNA. Translation: AAB02268.1.
U82664 Genomic DNA. Translation: AAB40238.1.
U00096 Genomic DNA. Translation: AAC73586.1.
AP009048 Genomic DNA. Translation: BAE76263.1.
PIRiC64779.
RefSeqiNP_415017.1. NC_000913.3.
WP_000083955.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliQ59385.
SMRiQ59385. Positions 4-164, 182-829.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261336. 9 interactions.
IntActiQ59385. 6 interactions.
STRINGi511145.b0484.

Protein family/group databases

TCDBi3.A.3.5.5. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbiQ59385.
PRIDEiQ59385.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73586; AAC73586; b0484.
BAE76263; BAE76263; BAE76263.
GeneIDi946106.
KEGGiecj:JW0473.
eco:b0484.
PATRICi32116127. VBIEscCol129921_0505.

Organism-specific databases

EchoBASEiEB3035.
EcoGeneiEG13246. copA.

Phylogenomic databases

eggNOGiENOG4105C59. Bacteria.
COG2217. LUCA.
HOGENOMiHOG000250397.
InParanoidiQ59385.
KOiK17686.
OMAiQDGSTDH.
PhylomeDBiQ59385.

Enzyme and pathway databases

BioCyciEcoCyc:G6260-MONOMER.
ECOL316407:JW0473-MONOMER.
MetaCyc:G6260-MONOMER.
SABIO-RKQ59385.

Miscellaneous databases

PROiQ59385.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HMA_dom.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 2 hits.
[Graphical view]
PRINTSiPR00120. HATPASE.
SUPFAMiSSF55008. SSF55008. 2 hits.
SSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOPA_ECOLI
AccessioniPrimary (citable) accession number: Q59385
Secondary accession number(s): P78245, Q2MBU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 148 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.