Reviewed, UniProtKB/Swiss-Prot Q47840 (COPZ_ENTHR)

Names and origin

Protein names

Recommended name:
    Copper chaperone copZ
Alternative name(s):
    Activator of copYZAB

Gene names

Name:

copZ

Organism

Enterococcus hirae

Taxonomic identifier

1354 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

Protein attributes

Sequence length	69 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Acts as a copper chaperone by delivering 2 Cu+ ions to copY Zn2+-bound form. This transfer results in displacement of zinc and dissociation of copY from the promoter, allowing transcription of the copYZAB operon. Ref.1 Ref.3 Ref.6
Subunit structure	Monomer in the absence of copper. Homodimer or homooligomer in the presence of copper ions. Interacts with the copper ATPase copA. Interacts with copY via a charge-based interaction. Ref.6 Ref.5 Ref.7
Subcellular location	Cytoplasm Probable.
Induction	By Cu+ and Cu2+. Ref.2
Miscellaneous	Controlled by copper-induced proteolysis.
Sequence similarities	Contains 1 HMA domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Copper Metal-binding
Molecular function	Chaperone
Technical term	3D-structure
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro copper ion transport Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW copper-exporting ATPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 69

69

Copper chaperone copZ

PRO_0000079248

Regions

Domain

2 – 68

67

HMA

Sites

Metal binding

12

1

Copper

Metal binding

15

1

Copper

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

69

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Beta strand

12 – 14

3

Helix

15 – 24

10

Beta strand

29 – 35

7

Turn

36 – 39

4

Beta strand

40 – 45

6

Turn

47 – 49

3

Helix

52 – 60

9

Beta strand

66 – 68

3

Sequences

	Sequence		Length	Mass (Da)
	Q47840-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 8BBCBFA4BD10C997	FASTA	69	7,653
	10 20 30 40 50 60 MKQEFSVKGM SCNHCVARIE EAVGRISGVK KVKVQLKKEK AVVKFDEANV QATEICQAIN ELGYQAEVI

References

[1]	"Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPases of Enterococcus hirae." Odermatt A., Solioz M. J. Biol. Chem. 270:4349-4354(1995) [PubMed: 7876197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459.
[2]	"Effects of promoter mutations on the in vivo regulation of the cop operon of Enterococcus hirae by copper(I) and copper(II)." Wunderli-Ye H., Solioz M. Biochem. Biophys. Res. Commun. 259:443-449(1999) [PubMed: 10362527] [Abstract] Cited for: INDUCTION BY COPPER. Strain: ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459.
[3]	"The Enterococcus hirae copper chaperone CopZ delivers copper(I) to the CopY repressor." Cobine P.A., Wickramasinghe W.A., Harrison M.D., Weber T., Solioz M., Dameron C.T. FEBS Lett. 445:27-30(1999) [PubMed: 10069368] [Abstract] Cited for: FUNCTION. Strain: ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459.
[4]	"Copper-induced proteolysis of the CopZ copper chaperone of Enterococcus hirae." Lu Z.H., Solioz M. J. Biol. Chem. 276:47822-47827(2001) [PubMed: 11585824] [Abstract] Cited for: REGULATION BY PROTEOLYSIS. Strain: ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459.
[5]	"Interaction of the CopZ copper chaperone with the CopA copper ATPase of Enterococcus hirae assessed by surface plasmon resonance." Multhaup G., Strausak D., Bissig K.-D., Solioz M. Biochem. Biophys. Res. Commun. 288:172-177(2001) [PubMed: 11594769] [Abstract] Cited for: INTERACTION WITH COPA. Strain: ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459.
[6]	"Copper transfer from the Cu(I) chaperone, CopZ, to the repressor, Zn(II)CopY: metal coordination environments and protein interactions." Cobine P.A., George G.N., Jones C.E., Wickramasinghe W.A., Solioz M., Dameron C.T. Biochemistry 41:5822-5829(2002) [PubMed: 11980486] [Abstract] Cited for: FUNCTION, INTERACTION WITH COPY. Strain: ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459.
[7]	"NMR structure and metal interactions of the CopZ copper chaperone." Wimmer R., Herrmann T., Solioz M., Wuethrich K. J. Biol. Chem. 274:22597-22603(1999) [PubMed: 10428839] [Abstract] Cited for: STRUCTURE BY NMR OF 3-69, SUBUNIT, COPPER BINDING. Strain: ATCC 8043 / DSM 20160 / JCM 8729 / LMG 6399 / NCIMB 6459.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z46807 Genomic DNA. Translation: CAA86836.1.

PIR

B56085.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CPZ	NMR	-	A	3-69	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR001877. ATPase1_Cu-transp.
IPR001757. ATPase_P-typ_ion-transptr.
IPR006122. Cu_ion_bd.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe_transpt.
[Graphical view]

PANTHER

PTHR11939. ATPase_P. 1 hit.

Pfam

PF00403. HMA. 1 hit.
[Graphical view]

PRINTS

PR00942. CUATPASEI.

TIGRFAMs

TIGR00003. Cu_ion_bd. 1 hit.

PROSITE

PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

COPZ_ENTHR

Accession

Primary (citable) accession number: Q47840

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)