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Protein
Submitted name:

Copper transporter CopA

Gene

copA

Organism
Escherichia coli O111:H- (strain 11128 / EHEC)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotation

Enzyme and pathway databases

BioCyciECOL585396:GJCW-531-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Copper transporter CopAImported
Gene namesi
Name:copAImported
Ordered Locus Names:ECO111_0519Imported
OrganismiEscherichia coli O111:H- (strain 11128 / EHEC)Imported
Taxonomic identifieri585396 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000001614 Componenti: Chromosome

Subcellular locationi

  • Cell membrane UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei185 – 20521HelicalUniRule annotationAdd
BLAST
Transmembranei217 – 23822HelicalUniRule annotationAdd
BLAST
Transmembranei245 – 26420HelicalUniRule annotationAdd
BLAST
Transmembranei284 – 30219HelicalUniRule annotationAdd
BLAST
Transmembranei436 – 45823HelicalUniRule annotationAdd
BLAST
Transmembranei464 – 48724HelicalUniRule annotationAdd
BLAST
Transmembranei778 – 79720HelicalUniRule annotationAdd
BLAST
Transmembranei803 – 82422HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Structurei

3D structure databases

ProteinModelPortaliC8UIR8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 6562HMAInterPro annotationAdd
BLAST
Domaini100 – 16364HMAInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]UniRule annotation
Contains 2 HMA domains.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helixUniRule annotation

Phylogenomic databases

HOGENOMiHOG000250397.
KOiK17686.
OMAiQDGSTDH.
OrthoDBiEOG6742RM.

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.

C8UIR8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQIIDLTLD 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 QKGEGESVHA 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
KAEAIKRLQS EGRQVAMVGD GINDAPALAQ ADVGIAMGGG SDVAIETAAI
760 770 780 790 800
TLMRHSLMGV ADALAISRAT LRNMKQNLLG AFIYNSIGIP VAAGILWPFT
810 820 830
GTLLNPVVAG AAMALSSITV VSNANRLLRF KPKE
Length:834
Mass (Da):87,937
Last modified:November 3, 2009 - v1
Checksum:i1FDAE23F11466931
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010960 Genomic DNA. Translation: BAI34496.1.
RefSeqiWP_000078269.1. NC_013364.1.

Genome annotation databases

EnsemblBacteriaiBAI34496; BAI34496; ECO111_0519.
KEGGieoi:ECO111_0519.
PATRICi32104096. VBIEscCol143187_0539.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010960 Genomic DNA. Translation: BAI34496.1.
RefSeqiWP_000078269.1. NC_013364.1.

3D structure databases

ProteinModelPortaliC8UIR8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAI34496; BAI34496; ECO111_0519.
KEGGieoi:ECO111_0519.
PATRICi32104096. VBIEscCol143187_0539.

Phylogenomic databases

HOGENOMiHOG000250397.
KOiK17686.
OMAiQDGSTDH.
OrthoDBiEOG6742RM.

Enzyme and pathway databases

BioCyciECOL585396:GJCW-531-MONOMER.

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...

Publicationsi

  1. "Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli."
    Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.
    Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 11128 / EHECImported.

Entry informationi

Entry nameiC8UIR8_ECO1A
AccessioniPrimary (citable) accession number: C8UIR8
Entry historyi
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: April 13, 2016
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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.