Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q48271

- COPP_HELPY

UniProt

Q48271 - COPP_HELPY

Protein

COP-associated protein

Gene

copP

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Part of a cation-transporting system which is associated with copper export out of the H.pylori cells.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi12 – 121Copper
    Metal bindingi15 – 151Copper

    GO - Molecular functioni

    1. copper ion binding Source: InterPro
    2. protein binding Source: IntAct

    GO - Biological processi

    1. copper ion transport Source: InterPro

    Keywords - Ligandi

    Copper, Metal-binding

    Enzyme and pathway databases

    BioCyciHPY:HP1073-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    COP-associated protein
    Alternative name(s):
    Copper ion-binding protein
    Gene namesi
    Name:copP
    Ordered Locus Names:HP_1073
    OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
    Taxonomic identifieri85962 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
    ProteomesiUP000000429: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 6666COP-associated proteinPRO_0000079246Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi12 ↔ 15Alternate1 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiQ48271.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rplNP560393EBI-7497456,EBI-7497678

    Protein-protein interaction databases

    DIPiDIP-3638N.
    IntActiQ48271. 4 interactions.
    MINTiMINT-161359.
    STRINGi85962.HP1073.

    Structurei

    Secondary structure

    1
    66
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 54
    Helixi14 – 2310
    Beta strandi26 – 3510
    Turni36 – 394
    Beta strandi40 – 456
    Helixi51 – 6111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YG0NMR-A1-66[»]
    ProteinModelPortaliQ48271.
    SMRiQ48271. Positions 1-66.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ48271.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 6665HMAPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 HMA domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2608.
    OMAiMKVTFQV.
    OrthoDBiEOG6742RM.

    Family and domain databases

    InterProiIPR000428. Cu-bd.
    IPR017969. Heavy-metal-associated_CS.
    IPR006121. HeavyMe-assoc_HMA.
    IPR006122. HMA_Cu_ion-bd.
    [Graphical view]
    PfamiPF00403. HMA. 1 hit.
    [Graphical view]
    PRINTSiPR00944. CUEXPORT.
    SUPFAMiSSF55008. SSF55008. 1 hit.
    TIGRFAMsiTIGR00003. TIGR00003. 1 hit.
    PROSITEiPS01047. HMA_1. 1 hit.
    PS50846. HMA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q48271-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKATFQVPSI TCNHCVDKIE KFVGEIEGVS FIDVSVEKKS VVVEFDAPAT   50
    QDLIKEALLD AGQEVV 66
    Length:66
    Mass (Da):7,196
    Last modified:November 1, 1997 - v2
    Checksum:i353E2C3D392816F1
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31A → V in strain: A68, NCTC 11638 and NCTC 11639.
    Natural varianti13 – 131N → D in strain: NCTC 11638.
    Natural varianti13 – 131N → S in strain: NCTC 11639.
    Natural varianti34 – 341V → A in strain: A68, NCTC 11638 and NCTC 11639.
    Natural varianti35 – 351S → N in strain: NCTC 11639.
    Natural varianti66 – 661V → I in strain: A68, NCTC 11638 and NCTC 11639.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59625 Genomic DNA. Translation: AAB05476.1.
    U97567 Genomic DNA. Translation: AAB66381.1.
    L33259 Genomic DNA. Translation: AAB67321.1.
    AE000511 Genomic DNA. Translation: AAD08120.1.
    PIRiA64654.
    RefSeqiNP_207864.1. NC_000915.1.
    YP_006934989.1. NC_018939.1.

    Genome annotation databases

    EnsemblBacteriaiAAD08120; AAD08120; HP_1073.
    GeneIDi13870267.
    899609.
    KEGGiheo:C694_05545.
    hpy:HP1073.
    PATRICi20593485. VBIHelPyl33062_1122.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59625 Genomic DNA. Translation: AAB05476.1 .
    U97567 Genomic DNA. Translation: AAB66381.1 .
    L33259 Genomic DNA. Translation: AAB67321.1 .
    AE000511 Genomic DNA. Translation: AAD08120.1 .
    PIRi A64654.
    RefSeqi NP_207864.1. NC_000915.1.
    YP_006934989.1. NC_018939.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YG0 NMR - A 1-66 [» ]
    ProteinModelPortali Q48271.
    SMRi Q48271. Positions 1-66.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-3638N.
    IntActi Q48271. 4 interactions.
    MINTi MINT-161359.
    STRINGi 85962.HP1073.

    Proteomic databases

    PRIDEi Q48271.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD08120 ; AAD08120 ; HP_1073 .
    GeneIDi 13870267.
    899609.
    KEGGi heo:C694_05545.
    hpy:HP1073.
    PATRICi 20593485. VBIHelPyl33062_1122.

    Phylogenomic databases

    eggNOGi COG2608.
    OMAi MKVTFQV.
    OrthoDBi EOG6742RM.

    Enzyme and pathway databases

    BioCyci HPY:HP1073-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q48271.

    Family and domain databases

    InterProi IPR000428. Cu-bd.
    IPR017969. Heavy-metal-associated_CS.
    IPR006121. HeavyMe-assoc_HMA.
    IPR006122. HMA_Cu_ion-bd.
    [Graphical view ]
    Pfami PF00403. HMA. 1 hit.
    [Graphical view ]
    PRINTSi PR00944. CUEXPORT.
    SUPFAMi SSF55008. SSF55008. 1 hit.
    TIGRFAMsi TIGR00003. TIGR00003. 1 hit.
    PROSITEi PS01047. HMA_1. 1 hit.
    PS50846. HMA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and membrane topology of a P type ATPase from Helicobacter pylori."
      Melchers K., Weitzenegger T., Buhmann A., Steinhilber W., Sachs G., Schaefer K.P.
      J. Biol. Chem. 271:446-457(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: A68.
    2. "Nucleotide sequence and mutational analysis indicate that two Helicobacter pylori genes encode a P-type ATPase and a cation-binding protein associated with copper transport."
      Ge Z., Hiratsuka K., Taylor D.E.
      Mol. Microbiol. 15:97-106(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 43629 / JCM 7656 / NCTC 11639 / UA802.
    3. "Identification and characterization of an operon of Helicobacter pylori that is involved in motility and stress adaptation."
      Beier D., Spohn G., Rappuoli R., Scarlato V.
      J. Bacteriol. 179:4676-4683(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DSM 4867 / CCUG 17874 / NCTC 11638.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700392 / 26695.
    5. "Structural insight into the distinct properties of copper transport by the Helicobacter pylori CopP protein."
      Park S.J., Jung Y.-S., Kim J.-S., Seo M.-D., Lee B.J.
      Proteins 71:1007-1019(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR IN COMPLEX WITH COPPER IONS, DISULFIDE BOND.

    Entry informationi

    Entry nameiCOPP_HELPY
    AccessioniPrimary (citable) accession number: Q48271
    Secondary accession number(s): O07682, Q48257
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Copper (2+) binding can oxidyze the Cys residues at the metal-binding site, leading to the formation of a disulfide bond.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Helicobacter pylori
      Helicobacter pylori (strain 26695): entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3