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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi13 – 131Copper
Metal bindingi16 – 161Copper

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131C → S: Loss of copper binding; when associated with S-16. 1 Publication
Mutagenesisi16 – 161C → S: Loss of copper binding; when associated with S-13. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6969Copper chaperone CopZPRO_0000079247Add
BLAST

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 interaction.
STRINGi224308.Bsubs1_010100018191.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Helixi14 – 2512Combined sources
Beta strandi30 – 367Combined sources
Turni37 – 404Combined sources
Beta strandi41 – 466Combined sources
Turni48 – 503Combined sources
Helixi53 – 6210Combined sources
Beta strandi67 – 693Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO32221.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 6967HMAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HMA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410681U. Bacteria.
ENOG410XUQ1. LUCA.
HOGENOMiHOG000038877.
InParanoidiO32221.
KOiK07213.
OMAiEGIIMEQ.
OrthoDBiEOG6742RM.
PhylomeDBiO32221.

Family and domain databases

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1K0VNMR-A1-69[»]
1P8GNMR-A1-69[»]
2QIFX-ray1.50A/B1-69[»]
3I9ZX-ray1.90A1-69[»]
ProteinModelPortaliO32221.
SMRiO32221. Positions 1-69.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO32221. 1 interaction.
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.
OrthoDBiEOG6742RM.
PhylomeDBiO32221.

Enzyme and pathway databases

BioCyciBSUB:BSU33510-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO32221.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "CopZ from Bacillus subtilis interacts in vivo with a copper exporting CPx-type ATPase CopA."
    Radford D.S., Kihlken M.A., Borrelly G.P.M., Harwood C.R., Le Brun N.E., Cavet J.S.
    FEMS Microbiol. Lett. 220:105-112(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COPA.
  3. "Two MerR homologues that affect copper induction of the Bacillus subtilis copZA operon."
    Gaballa A., Cao M., Helmann J.D.
    Microbiology 149:3413-3421(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REGULATION.
  4. "Copper-mediated dimerization of CopZ, a predicted copper chaperone from Bacillus subtilis."
    Kihlken M.A., Leech A.P., Le Brun N.E.
    Biochem. J. 368:729-739(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH COPPER IONS, MUTAGENESIS OF CYS-13 AND CYS-16, SUBUNIT.
  5. "X-ray absorption and NMR spectroscopic studies of CopZ, a copper chaperone in Bacillus subtilis: the coordination properties of the copper ion."
    Banci L., Bertini I., Del Conte R., Mangani S., Meyer-Klaucke W.
    Biochemistry 42:2467-2474(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR IN COMPLEX WITH COPPER IONS, SUBUNIT.
  6. "Solution structure of apo CopZ from Bacillus subtilis: further analysis of the changes associated with the presence of copper."
    Banci L., Bertini I., Del Conte R.
    Biochemistry 42:13422-13428(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

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: February 17, 2016
This is version 115 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.