copZ

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)

Length

204 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) directly to the transmembrane transport sites of copper-exporting P-type ATPase A (CopA). Probably has a redox function due to the presence of a 2Fe-2S cluster and could reduce Cu(2+) to Cu(+).

Mass

22.588 kDa

Sequence

MMRCPECSTEGWRVLPLTVGAHVKEGLWSKIKGDFYFCSLESCEVVYFNEQTVFRKGELKTRVGVKEREEPKPVCYCNRVTEKMLLEAAEKFGKEKAVEITGAGKGKWCVVTNPSGRCCHWHLERLGFPVGGEKKAAKRVEIKLDGLTCMGCVSAVKAALEEAGANVVEIGLDRAVVEVDEEAELQKLVEAVEGAGYSARLEKR

Protein

Copper chaperone CopZ: copZ

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)

Length

204 amino acids

Function

Mass

22.588 kDa

Sequence

Protein

Copper chaperone CopZ: copZ

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Bacillus subtilis (strain 168)

Length

69 amino acids

Function

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).

Mass

7.338 kDa

Sequence

MEQKTLQVEGMSCQHCVKAVETSVGELDGVSAVHVNLEAGKVDVSFDADKVSVKDIADAIEDQGYDVAK

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)

Length

69 amino acids

Function

Acts as a copper chaperone by delivering 2 Cu(+) ions to CopY Zn(2+)-bound form. This transfer results in displacement of zinc and dissociation of CopY from the promoter, allowing transcription of the copYZAB operon.

Mass

7.653 kDa

Sequence

MKQEFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEANVQATEICQAINELGYQAEVI

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Bacillus subtilis (strain 168)

Length

69 amino acids

Function

Mass

7.338 kDa

Sequence

MEQKTLQVEGMSCQHCVKAVETSVGELDGVSAVHVNLEAGKVDVSFDADKVSVKDIADAIEDQGYDVAK

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258)

Length

69 amino acids

Function

Mass

7.653 kDa

Sequence

MKQEFSVKGMSCNHCVARIEEAVGRISGVKKVKVQLKKEKAVVKFDEANVQATEICQAINELGYQAEVI

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus aureus (strain Mu3 / ATCC 700698)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.237 kDa

Sequence

MSQEILNVEGMSCGHCKSAVESALNNIDGVTSADVNLENGQVSVQYDDSKVAVSQMKDAIEDQGYDVV

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus aureus (strain JH1)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.237 kDa

Sequence

MSQEILNVEGMSCGHCKSAVESALNNIDGVTSADVNLENGQVSVQYDDSKVAVSQMKDAIEDQGYDVV

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus aureus (strain USA300)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.237 kDa

Sequence

MSQEILNVEGMSCGHCKSAVESALNNIDGVTSADVNLENGQVSVQYDDSKVAVSQMKDAIEDQGYDVV

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus aureus (strain NCTC 8325)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.237 kDa

Sequence

MSQEILNVEGMSCGHCKSAVESALNNIDGVTSADVNLENGQVSVQYDDSKVAVSQMKDAIEDQGYDVV

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus aureus (strain JH9)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.237 kDa

Sequence

MSQEILNVEGMSCGHCKSAVESALNNIDGVTSADVNLENGQVSVQYDDSKVAVSQMKDAIEDQGYDVV

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus aureus (strain bovine RF122 / ET3-1)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.251 kDa

Sequence

MSQEILNVEGMSCGHCKSAVESALNNIDGVTSAEVNLENGQVSVQYDDSKVAVSQMKDAIEDQGYDVV

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus aureus (strain COL)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.237 kDa

Sequence

MSQEILNVEGMSCGHCKSAVESALNNIDGVTSADVNLENGQVSVQYDDSKVAVSQMKDAIEDQGYDVV

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus aureus (strain Newman)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.237 kDa

Sequence

MSQEILNVEGMSCGHCKSAVESALNNIDGVTSADVNLENGQVSVQYDDSKVAVSQMKDAIEDQGYDVV

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus aureus (strain Mu50 / ATCC 700699)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.237 kDa

Sequence

MSQEILNVEGMSCGHCKSAVESALNNIDGVTSADVNLENGQVSVQYDDSKVAVSQMKDAIEDQGYDVV

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus aureus (strain N315)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.237 kDa

Sequence

MSQEILNVEGMSCGHCKSAVESALNNIDGVTSADVNLENGQVSVQYDDSKVAVSQMKDAIEDQGYDVV

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus aureus (strain MRSA252)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.251 kDa

Sequence

MSQEILNVEGMSCGHCKSAVESALNNIDGVTSAEVNLENGQVSVQYDDSKVAVSQMKDAIEDQGYDVV

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus aureus (strain MSSA476)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.237 kDa

Sequence

MSQEILNVEGMSCGHCKSAVESALNNIDGVTSADVNLENGQVSVQYDDSKVAVSQMKDAIEDQGYDVV

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus aureus (strain USA300 / TCH1516)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.237 kDa

Sequence

MSQEILNVEGMSCGHCKSAVESALNNIDGVTSADVNLENGQVSVQYDDSKVAVSQMKDAIEDQGYDVV

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus aureus (strain MW2)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.237 kDa

Sequence

MSQEILNVEGMSCGHCKSAVESALNNIDGVTSADVNLENGQVSVQYDDSKVAVSQMKDAIEDQGYDVV

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus epidermidis (strain ATCC 35984 / RP62A)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.661 kDa

Sequence

MTQKIIKVEGMSCEHCRNAVESALAKLNGVSSAEVNLDENHVRVEYNDSKVTFENMKEAIEEQGYDVK

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus epidermidis (strain ATCC 12228)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.661 kDa

Sequence

MTQKIIKVEGMSCEHCRNAVESALAKLNGVSSAEVNLDENHVRVEYNDSKVTFENMKEAIEEQGYDVK

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus haemolyticus (strain JCSC1435)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.615 kDa

Sequence

MINKVINVEGMSCDHCRNAVESALAKLNGVTSAEVDLDKNQVRVDYDENRVSVEQMKEAIEDQGYDVK

Gene

copZ

Protein

Copper chaperone CopZ

Organism

Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41)

Length

68 amino acids

Function

Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-exporting P-type ATPase A (CopA) (By similarity).

Mass

7.377 kDa

Sequence

MATETIQVEGMSCDHCKHAVETALTELDGVSTADVSLEAGNVKVDFDDDKVTMPQMKDAIEDQGYDVK