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Protein

Copper chaperone CopZ

Gene

copZ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi13Copper1
Metal bindingi16Copper1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Copper, 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
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.

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

Sequence similaritiesi

Contains 1 HMA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410681U. Bacteria.
ENOG410XUQ1. LUCA.
HOGENOMiHOG000038877.
InParanoidiO32221.
KOiK07213.
OMAiEGIIMEQ.
PhylomeDBiO32221.

Family and domain databases

CDDicd00371. HMA. 1 hit.
InterProiIPR000428. Cu-bd.
IPR017969. Heavy-metal-associated_CS.
IPR006122. HMA_Cu_ion-bd.
IPR006121. HMA_dom.
[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.

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.
PATRICi18978704. VBIBacSub10457_3515.

Cross-referencesi

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.

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...

Protein-protein interaction databases

IntActiO32221. 1 interactor.
STRINGi224308.Bsubs1_010100018191.

Proteomic databases

PaxDbiO32221.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15356; CAB15356; BSU33510.
GeneIDi937974.
KEGGibsu:BSU33510.
PATRICi18978704. VBIBacSub10457_3515.

Phylogenomic databases

eggNOGiENOG410681U. Bacteria.
ENOG410XUQ1. LUCA.
HOGENOMiHOG000038877.
InParanoidiO32221.
KOiK07213.
OMAiEGIIMEQ.
PhylomeDBiO32221.

Enzyme and pathway databases

BioCyciBSUB:BSU33510-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO32221.

Family and domain databases

CDDicd00371. HMA. 1 hit.
InterProiIPR000428. Cu-bd.
IPR017969. Heavy-metal-associated_CS.
IPR006122. HMA_Cu_ion-bd.
IPR006121. HMA_dom.
[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]
ProtoNetiSearch...

Entry informationi

Entry nameiCOPZ_BACSU
AccessioniPrimary (citable) accession number: O32221
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

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
  3. 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.