COPZ_BACSU
ID COPZ_BACSU Reviewed; 69 AA.
AC O32221;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Copper chaperone CopZ;
DE AltName: Full=Copper-ion-binding protein;
GN Name=copZ; Synonyms=yvgY; OrderedLocusNames=BSU33510;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP INTERACTION WITH COPA.
RX PubMed=12644235; DOI=10.1016/s0378-1097(03)00095-8;
RA Radford D.S., Kihlken M.A., Borrelly G.P.M., Harwood C.R., Le Brun N.E.,
RA Cavet J.S.;
RT "CopZ from Bacillus subtilis interacts in vivo with a copper exporting CPx-
RT type ATPase CopA.";
RL FEMS Microbiol. Lett. 220:105-112(2003).
RN [3]
RP REGULATION.
RX PubMed=14663075; DOI=10.1099/mic.0.26225-0;
RA Gaballa A., Cao M., Helmann J.D.;
RT "Two MerR homologues that affect copper induction of the Bacillus subtilis
RT copZA operon.";
RL Microbiology 149:3413-3421(2003).
RN [4]
RP FUNCTION AS A CHAPERONE.
RX PubMed=25899340; DOI=10.1111/mmi.13038;
RA Drees S.L., Beyer D.F., Lenders-Lomscher C., Luebben M.;
RT "Distinct functions of serial metal-binding domains in the Escherichia coli
RT P1 B-ATPase CopA.";
RL Mol. Microbiol. 97:423-438(2015).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH COPPER IONS,
RP MUTAGENESIS OF CYS-13 AND CYS-16, AND SUBUNIT.
RX PubMed=12238948; DOI=10.1042/bj20021036;
RA Kihlken M.A., Leech A.P., Le Brun N.E.;
RT "Copper-mediated dimerization of CopZ, a predicted copper chaperone from
RT Bacillus subtilis.";
RL Biochem. J. 368:729-739(2002).
RN [6]
RP STRUCTURE BY NMR IN COMPLEX WITH COPPER IONS, AND SUBUNIT.
RX PubMed=12600214; DOI=10.1021/bi0205810;
RA Banci L., Bertini I., Del Conte R., Mangani S., Meyer-Klaucke W.;
RT "X-ray absorption and NMR spectroscopic studies of CopZ, a copper chaperone
RT in Bacillus subtilis: the coordination properties of the copper ion.";
RL Biochemistry 42:2467-2474(2003).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=14621987; DOI=10.1021/bi0353326;
RA Banci L., Bertini I., Del Conte R.;
RT "Solution structure of apo CopZ from Bacillus subtilis: further analysis of
RT the changes associated with the presence of copper.";
RL Biochemistry 42:13422-13428(2003).
CC -!- FUNCTION: Chaperone that serves for the intracellular sequestration and
CC transport of Cu(+). Delivers Cu(+) to the copper-transporting ATPase
CC CopA. Functions in E.coli to transfer Cu(+) to CopA missing its first
CC metal-binding domain (PubMed:25899340). {ECO:0000269|PubMed:25899340}.
CC -!- SUBUNIT: Monomer in the absence of copper. Homodimer in the presence of
CC copper ions. Forms a heterodimer (electrostatic interactions) with CopA
CC during the transfer of Cu(+). {ECO:0000269|PubMed:12238948,
CC ECO:0000269|PubMed:12600214}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By Cu(2+).
CC -!- MISCELLANEOUS: The copZA operon is activated by CueR and indirectly
CC repressed by YfmP.
CC -!- MISCELLANEOUS: Cu(+) ion is always at least three-coordinated.
CC Physiological thiol may be needed to complete the Cu(+) coordination
CC sphere in order to prevent homodimer (dead-end products) formation
CC between 2 CopZ.
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DR EMBL; AL009126; CAB15356.1; -; Genomic_DNA.
DR PIR; F70041; F70041.
DR RefSeq; NP_391231.1; NC_000964.3.
DR RefSeq; WP_003244260.1; NZ_JNCM01000033.1.
DR PDB; 1K0V; NMR; -; A=1-69.
DR PDB; 1P8G; NMR; -; A=1-69.
DR PDB; 2QIF; X-ray; 1.50 A; A/B=1-69.
DR PDB; 3I9Z; X-ray; 1.90 A; A=1-69.
DR PDBsum; 1K0V; -.
DR PDBsum; 1P8G; -.
DR PDBsum; 2QIF; -.
DR PDBsum; 3I9Z; -.
DR AlphaFoldDB; O32221; -.
DR BMRB; O32221; -.
DR SMR; O32221; -.
DR IntAct; O32221; 1.
DR STRING; 224308.BSU33510; -.
DR jPOST; O32221; -.
DR PaxDb; O32221; -.
DR PRIDE; O32221; -.
DR EnsemblBacteria; CAB15356; CAB15356; BSU_33510.
DR GeneID; 937974; -.
DR KEGG; bsu:BSU33510; -.
DR PATRIC; fig|224308.179.peg.3636; -.
DR eggNOG; COG2608; Bacteria.
DR InParanoid; O32221; -.
DR OMA; HCVNAIT; -.
DR PhylomeDB; O32221; -.
DR BioCyc; BSUB:BSU33510-MON; -.
DR EvolutionaryTrace; O32221; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0006825; P:copper ion transport; IEA:InterPro.
DR CDD; cd00371; HMA; 1.
DR InterPro; IPR000428; Cu-bd.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006122; HMA_Cu_ion-bd.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR Pfam; PF00403; HMA; 1.
DR PRINTS; PR00944; CUEXPORT.
DR SUPFAM; SSF55008; SSF55008; 1.
DR TIGRFAMs; TIGR00003; TIGR00003; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Copper; Cytoplasm; Metal-binding;
KW Reference proteome.
FT CHAIN 1..69
FT /note="Copper chaperone CopZ"
FT /id="PRO_0000079247"
FT DOMAIN 2..68
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 13
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 16
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT MUTAGEN 13
FT /note="C->S: Loss of copper binding; when associated with
FT S-16."
FT /evidence="ECO:0000269|PubMed:12238948"
FT MUTAGEN 16
FT /note="C->S: Loss of copper binding; when associated with
FT S-13."
FT /evidence="ECO:0000269|PubMed:12238948"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:2QIF"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:2QIF"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:2QIF"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:2QIF"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:2QIF"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2QIF"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:2QIF"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1K0V"
SQ SEQUENCE 69 AA; 7338 MW; 43F95461AE4B5497 CRC64;
MEQKTLQVEG MSCQHCVKAV ETSVGELDGV SAVHVNLEAG KVDVSFDADK VSVKDIADAI
EDQGYDVAK
