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Protein

Copper chaperone CopZ

Gene

copZ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Chaperone that serves for the intracellular sequestration and transport of Cu+. Delivers Cu+ to the copper-transporting ATPase CopA. Functions in E.coli to transfer Cu+ to CopA missing its first metal-binding domain (PubMed:25899340).1 Publication

Miscellaneous

The copZA operon is activated by CueR and indirectly repressed by YfmP.
Cu+ ion is always at least three-coordinated. Physiological thiol may be needed to complete the Cu+ coordination sphere in order to prevent homodimer (dead-end products) formation between 2 CopZ.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi13Copper1
Metal bindingi16Copper1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone
LigandCopper, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU33510-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Copper chaperone CopZ
Alternative name(s):
Copper-ion-binding protein
Gene namesi
Name:copZ
Synonyms:yvgY
Ordered Locus Names:BSU33510
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi13C → S: Loss of copper binding; when associated with S-16. 1 Publication1
Mutagenesisi16C → S: Loss of copper binding; when associated with S-13. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000792471 – 69Copper chaperone CopZAdd BLAST69

Proteomic databases

PaxDbiO32221
PRIDEiO32221

Expressioni

Inductioni

By Cu2+.

Interactioni

Subunit structurei

Monomer in the absence of copper. Homodimer in the presence of copper ions. Forms a heterodimer (electrostatic interactions) with CopA during the transfer of Cu+.2 Publications

Protein-protein interaction databases

IntActiO32221, 1 interactor
STRINGi224308.Bsubs1_010100018191

Structurei

Secondary structure

169
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 9Combined sources8
Helixi14 – 25Combined sources12
Beta strandi30 – 36Combined sources7
Turni37 – 40Combined sources4
Beta strandi41 – 46Combined sources6
Turni48 – 50Combined sources3
Helixi53 – 62Combined sources10
Beta strandi67 – 69Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K0VNMR-A1-69[»]
1P8GNMR-A1-69[»]
2QIFX-ray1.50A/B1-69[»]
3I9ZX-ray1.90A1-69[»]
ProteinModelPortaliO32221
SMRiO32221
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO32221

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 69HMAPROSITE-ProRule annotationAdd BLAST67

Phylogenomic databases

eggNOGiENOG410681U Bacteria
ENOG410XUQ1 LUCA
HOGENOMiHOG000038877
InParanoidiO32221
KOiK07213
OMAiEGIIMEQ
PhylomeDBiO32221

Family and domain databases

CDDicd00371 HMA, 1 hit
InterProiView protein in InterPro
IPR000428 Cu-bd
IPR017969 Heavy-metal-associated_CS
IPR006122 HMA_Cu_ion-bd
IPR006121 HMA_dom
IPR036163 HMA_dom_sf
PfamiView protein in Pfam
PF00403 HMA, 1 hit
PRINTSiPR00944 CUEXPORT
SUPFAMiSSF55008 SSF55008, 1 hit
TIGRFAMsiTIGR00003 TIGR00003, 1 hit
PROSITEiView protein in PROSITE
PS01047 HMA_1, 1 hit
PS50846 HMA_2, 1 hit

Sequencei

Sequence statusi: Complete.

O32221-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQKTLQVEG MSCQHCVKAV ETSVGELDGV SAVHVNLEAG KVDVSFDADK
60
VSVKDIADAI EDQGYDVAK
Length:69
Mass (Da):7,338
Last modified:January 1, 1998 - v1
Checksum:i43F95461AE4B5497
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA Translation: CAB15356.1
PIRiF70041
RefSeqiNP_391231.1, NC_000964.3
WP_003244260.1, NZ_JNCM01000033.1

Genome annotation databases

EnsemblBacteriaiCAB15356; CAB15356; BSU33510
GeneIDi937974
KEGGibsu:BSU33510
PATRICifig|224308.179.peg.3636

Entry informationi

Entry nameiCOPZ_BACSU
AccessioniPrimary (citable) accession number: O32221
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 1, 1998
Last modified: May 23, 2018
This is version 123 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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