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Protein

Probable copper-importing P-type ATPase A

Gene

copA

Organism
Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probably involved in copper import under copper limiting conditions.2 Publications

Catalytic activityi

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

Enzyme regulationi

Inhibited by vanadate.1 Publication

Kineticsi

  1. KM=0.2 mM for ATP1 Publication
  1. Vmax=0.15 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 6.25.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi17CopperPROSITE-ProRule annotation1
Metal bindingi20CopperPROSITE-ProRule annotation1
Active sitei4254-aspartylphosphate intermediateBy similarity1
Metal bindingi621MagnesiumPROSITE-ProRule annotation1
Metal bindingi625MagnesiumPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

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

SABIO-RKP32113.

Protein family/group databases

TCDBi3.A.3.5.1. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable copper-importing P-type ATPase A (EC:3.6.3.54)
Gene namesi
Name:copA
Ordered Locus Names:EHR_09085
OrganismiEnterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)
Taxonomic identifieri768486 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
Proteomesi
  • UP000002895 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 94CytoplasmicSequence analysisAdd BLAST94
Transmembranei95 – 115HelicalSequence analysisAdd BLAST21
Topological domaini116 – 119ExtracellularSequence analysis4
Transmembranei120 – 137HelicalSequence analysisAdd BLAST18
Topological domaini138 – 161CytoplasmicSequence analysisAdd BLAST24
Transmembranei162 – 181HelicalSequence analysisAdd BLAST20
Topological domaini182 – 187ExtracellularSequence analysis6
Transmembranei188 – 203HelicalSequence analysisAdd BLAST16
Topological domaini204 – 341CytoplasmicSequence analysisAdd BLAST138
Transmembranei342 – 362HelicalSequence analysisAdd BLAST21
Topological domaini363 – 375ExtracellularSequence analysisAdd BLAST13
Transmembranei376 – 396HelicalSequence analysisAdd BLAST21
Topological domaini397 – 678CytoplasmicSequence analysisAdd BLAST282
Transmembranei679 – 698HelicalSequence analysisAdd BLAST20
Topological domaini699 – 700ExtracellularSequence analysis2
Transmembranei701 – 721HelicalSequence analysisAdd BLAST21
Topological domaini722 – 727CytoplasmicSequence analysis6

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi17C → S: Still strongly interacts with CopZ but abolishes the modulating activity of copper; when associated with S-20. 1 Publication1
Mutagenesisi20C → S: Still strongly interacts with CopZ but abolishes the modulating activity of copper; when associated with S-17. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000462501 – 727Probable copper-importing P-type ATPase AAdd BLAST727

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP32113.

Expressioni

Inductioni

By copper and silver.1 Publication

Interactioni

Subunit structurei

Monomer. Interacts with the copper chaperone CopZ.1 Publication

Protein-protein interaction databases

MINTiMINT-219443.

Structurei

3D structure databases

ProteinModelPortaliP32113.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 71HMAPROSITE-ProRule annotationAdd BLAST65

Sequence similaritiesi

Contains 1 HMA domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK17686.
OrthoDBiPOG091H00YH.

Family and domain databases

CDDicd00371. HMA. 1 hit.
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. 1 hit.
[Graphical view]
SUPFAMiSSF55008. SSF55008. 1 hit.
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. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32113-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATNTKMETF VITGMTCANC SARIEKELNE QPGVMSATVN LATEKASVKY
60 70 80 90 100
TDTTTERLIK SVENIGYGAI LYDEAHKQKI AEEKQTYLRK MKFDLIFSAI
110 120 130 140 150
LTLPLMLAMI AMMLGSHGPI VSFFHLSLVQ LLFALPVQFY VGWRFYKGAY
160 170 180 190 200
HALKTKAPNM DVLVAIGTSA AFALSIYNGF FPSHSHDLYF ESSSMIITLI
210 220 230 240 250
LLGKYLEHTA KSKTGDAIKQ MMSLQTKTAQ VLRDGKEETI AIDEVMIDDI
260 270 280 290 300
LVIRPGEQVP TDGRIIAGTS ALDESMLTGE SVPVEKKEKD MVFGGTINTN
310 320 330 340 350
GLIQIQVSQI GKDTVLAQII QMVEDAQGSK APIQQIADKI SGIFVPIVLF
360 370 380 390 400
LALVTLLVTG WLTKDWQLAL LHSVSVLVIA CPCALGLATP TAIMVGTGVG
410 420 430 440 450
AHNGILIKGG EALEGAAHLN SIILDKTGTI TQGRPEVTDV IGPKEIISLF
460 470 480 490 500
YSLEHASEHP LGKAIVAYGA KVGAKTQPIT DFVAHPGAGI SGTINGVHYF
510 520 530 540 550
AGTRKRLAEM NLSFDEFQEQ ALELEQAGKT VMFLANEEQV LGMIAVADQI
560 570 580 590 600
KEDAKQAIEQ LQQKGVDVFM VTGDNQRAAQ AIGKQVGIDS DHIFAEVLPE
610 620 630 640 650
EKANYVEKLQ KAGKKVGMVG DGINDAPALA LADVGIAMGS GTDIAMETAD
660 670 680 690 700
VTLMNSHLTS INQMISLSAA TLKKIKQNLF WAFIYNTIGI PFAAFGFLNP
710 720
IIAGGAMAFS SISVLLNSLS LNRKTIK
Length:727
Mass (Da):78,303
Last modified:January 9, 2013 - v2
Checksum:i30A0858F2389B22B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti630A → R in AAA61835 (PubMed:8048974).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13292 Genomic DNA. Translation: AAA61835.1.
CP003504 Genomic DNA. Translation: AFM70729.1.
Z46807 Genomic DNA. Translation: CAA86837.1.
PIRiA45995.
RefSeqiWP_010737925.1. NZ_KB946231.1.

Genome annotation databases

EnsemblBacteriaiAFM70729; AFM70729; EHR_09085.
GeneIDi13177746.
KEGGiehr:EHR_09085.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13292 Genomic DNA. Translation: AAA61835.1.
CP003504 Genomic DNA. Translation: AFM70729.1.
Z46807 Genomic DNA. Translation: CAA86837.1.
PIRiA45995.
RefSeqiWP_010737925.1. NZ_KB946231.1.

3D structure databases

ProteinModelPortaliP32113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-219443.

Protein family/group databases

TCDBi3.A.3.5.1. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PRIDEiP32113.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFM70729; AFM70729; EHR_09085.
GeneIDi13177746.
KEGGiehr:EHR_09085.

Phylogenomic databases

KOiK17686.
OrthoDBiPOG091H00YH.

Enzyme and pathway databases

SABIO-RKP32113.

Family and domain databases

CDDicd00371. HMA. 1 hit.
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. 1 hit.
[Graphical view]
SUPFAMiSSF55008. SSF55008. 1 hit.
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. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOPA_ENTHA
AccessioniPrimary (citable) accession number: P32113
Secondary accession number(s): I6TBM0, Q47841
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 9, 2013
Last modified: November 30, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.