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Cadmium resistance transcriptional regulatory protein CadC (Cadmium efflux system accessory protein)

 CADC_STAAU              Reviewed;         122 AA.
P20047;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
25-OCT-2017, entry version 92.
RecName: Full=Cadmium resistance transcriptional regulatory protein CadC;
AltName: Full=Cadmium efflux system accessory protein;
Name=cadC;
Staphylococcus aureus.
Plasmid pI258.
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
Staphylococcus.
NCBI_TaxID=1280;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2524829; DOI=10.1073/pnas.86.10.3544;
Nucifora G., Chu L., Misra T.K., Silver S.;
"Cadmium resistance from Staphylococcus aureus plasmid pI258 cadA gene
results from a cadmium-efflux ATPase.";
Proc. Natl. Acad. Sci. U.S.A. 86:3544-3548(1989).
[2]
IDENTIFICATION.
PubMed=1938959; DOI=10.1128/jb.173.23.7636-7642.1991;
Yoon K.P., Silver S.;
"A second gene in the Staphylococcus aureus cadA cadmium resistance
determinant of plasmid pI258.";
J. Bacteriol. 173:7636-7642(1991).
[3]
FUNCTION, AND DNA-BINDING.
PubMed=7543476; DOI=10.1128/jb.177.15.4437-4441.1995;
Endo G., Silver S.;
"CadC, the transcriptional regulatory protein of the cadmium
resistance system of Staphylococcus aureus plasmid pI258.";
J. Bacteriol. 177:4437-4441(1995).
[4]
FUNCTION, AND MUTAGENESIS OF CYS-7; CYS-11; CYS-58 AND CYS-60.
PubMed=11278706; DOI=10.1074/jbc.M010595200;
Sun Y., Wong M.D., Rosen B.P.;
"Role of cysteinyl residues in sensing Pb(II), Cd(II), and Zn(II) by
the plasmid pI258 CadC repressor.";
J. Biol. Chem. 276:14955-14960(2001).
[5]
FUNCTION, SUBUNIT, MUTAGENESIS OF HIS-103, AND METAL BINDING SITES.
PubMed=12176999; DOI=10.1074/jbc.M206536200;
Wong M.D., Lin Y.-F., Rosen B.P.;
"The soft metal ion binding sites in the Staphylococcus aureus pI258
CadC Cd(II)/Pb(II)/Zn(II)-responsive repressor are formed between
subunits of the homodimer.";
J. Biol. Chem. 277:40930-40936(2002).
[6]
FUNCTION, AND SUBUNIT.
PubMed=11941514; DOI=10.1007/s00775-001-0336-9;
Busenlehner L.S., Apuy J.L., Giedroc D.P.;
"Characterization of a metalloregulatory bismuth(III) site in
Staphylococcus aureus pI258 CadC repressor.";
J. Biol. Inorg. Chem. 7:551-559(2002).
[7]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ZINC IONS, AND
SUBUNIT.
PubMed=15937183; DOI=10.1128/JB.187.12.4214-4221.2005;
Ye J., Kandegedara A., Martin P., Rosen B.P.;
"Crystal structure of the Staphylococcus aureus pI258 CadC
Cd(II)/Pb(II)/Zn(II)-responsive repressor.";
J. Bacteriol. 187:4214-4221(2005).
[8]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH METAL IONS,
FUNCTION, CHARACTERIZATION OF METAL BINDING SITES, SUBUNIT, AND
MUTAGENESIS OF CYS-7; CYS-11; CYS-58; CYS-60; ASP-101 AND HIS-103.
PubMed=19286656; DOI=10.1074/jbc.M809179200;
Kandegedara A., Thiyagarajan S., Kondapalli K.C., Stemmler T.L.,
Rosen B.P.;
"Role of bound Zn(II) in the CadC Cd(II)/Pb(II)/Zn(II)-responsive
repressor.";
J. Biol. Chem. 284:14958-14965(2009).
-!- FUNCTION: Metal-binding repressor for the cad operon. Involved in
resistance to heavy metals, such as cadmium, bismuth, zinc or
lead. Binds 2 metal ions per subunit. Metal binding to the N-
terminal regulatory site causes the repressor to dissociate from
the DNA. {ECO:0000269|PubMed:11278706,
ECO:0000269|PubMed:11941514, ECO:0000269|PubMed:12176999,
ECO:0000269|PubMed:19286656, ECO:0000269|PubMed:7543476}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11941514,
ECO:0000269|PubMed:12176999, ECO:0000269|PubMed:15937183,
ECO:0000269|PubMed:19286656}.
-!- MISCELLANEOUS: The N-terminal, regulatory metal binding site 1 has
higher affinity for cadmium than for zinc. The second metal
binding site has higher affinity for zinc and has no regulatory
function.
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EMBL; J04551; AAB59153.1; -; Genomic_DNA.
PIR; B32561; B32561.
RefSeq; WP_000726007.1; NZ_NKCQ01000010.1.
RefSeq; YP_006937601.1; NC_013319.1.
RefSeq; YP_006937788.1; NC_013323.1.
RefSeq; YP_006938262.1; NC_013337.1.
RefSeq; YP_006938636.1; NC_013347.1.
RefSeq; YP_006938769.1; NC_013352.1.
PDB; 1U2W; X-ray; 1.90 A; A/B/C/D=1-122.
PDB; 3F72; X-ray; 2.31 A; A/B/C/D/E/F=1-122.
PDBsum; 1U2W; -.
PDBsum; 3F72; -.
ProteinModelPortal; P20047; -.
SMR; P20047; -.
GeneID; 13874749; -.
GeneID; 13874940; -.
GeneID; 13875429; -.
GeneID; 13875813; -.
GeneID; 13875978; -.
EvolutionaryTrace; P20047; -.
GO; GO:0005622; C:intracellular; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro.
GO; GO:0046686; P:response to cadmium ion; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00090; HTH_ARSR; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR011991; ArsR-like_HTH.
InterPro; IPR018334; ArsR_HTH.
InterPro; IPR001845; HTH_ArsR_DNA-bd_dom.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF01022; HTH_5; 1.
PRINTS; PR00778; HTHARSR.
SMART; SM00418; HTH_ARSR; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS00846; HTH_ARSR_1; 1.
PROSITE; PS50987; HTH_ARSR_2; 1.
1: Evidence at protein level;
3D-structure; Cadmium; Cadmium resistance; DNA-binding; Metal-binding;
Plasmid; Transcription; Transcription regulation; Zinc.
CHAIN 1 122 Cadmium resistance transcriptional
regulatory protein CadC.
/FTId=PRO_0000160620.
DOMAIN 24 119 HTH arsR-type. {ECO:0000255|PROSITE-
ProRule:PRU00340}.
DNA_BIND 59 78 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00340}.
METAL 7 7 Cadmium; shared with dimeric partner.
METAL 11 11 Cadmium; shared with dimeric partner.
METAL 58 58 Cadmium; shared with dimeric partner.
METAL 60 60 Cadmium; shared with dimeric partner.
METAL 101 101 Zinc; shared with dimeric partner.
METAL 103 103 Zinc; shared with dimeric partner.
METAL 114 114 Zinc; shared with dimeric partner.
METAL 117 117 Zinc; shared with dimeric partner.
MUTAGEN 7 7 C->S: Abolishes dissociation from DNA;
when associated with G-11; S-58 and S-60.
{ECO:0000269|PubMed:11278706,
ECO:0000269|PubMed:19286656}.
MUTAGEN 11 11 C->G: No effect. Abolishes dissociation
from DNA; when associated with S-7; S-58
and S-60. {ECO:0000269|PubMed:11278706,
ECO:0000269|PubMed:19286656}.
MUTAGEN 58 58 C->S: Abolishes dissociation from DNA;
when associated with S-7; G-11 and S-60.
{ECO:0000269|PubMed:11278706,
ECO:0000269|PubMed:19286656}.
MUTAGEN 60 60 C->S: Abolishes dissociation from DNA;
when associated with S-7; G-11 and S-58.
{ECO:0000269|PubMed:11278706,
ECO:0000269|PubMed:19286656}.
MUTAGEN 101 101 D->G: No effect on repressor activity;
when associated with A-103.
{ECO:0000269|PubMed:19286656}.
MUTAGEN 103 103 H->A: No effect on repressor activity;
when associated with G-101.
{ECO:0000269|PubMed:12176999,
ECO:0000269|PubMed:19286656}.
STRAND 11 13 {ECO:0000244|PDB:3F72}.
HELIX 14 25 {ECO:0000244|PDB:1U2W}.
TURN 26 28 {ECO:0000244|PDB:1U2W}.
HELIX 29 40 {ECO:0000244|PDB:1U2W}.
HELIX 42 53 {ECO:0000244|PDB:1U2W}.
HELIX 59 66 {ECO:0000244|PDB:1U2W}.
HELIX 70 82 {ECO:0000244|PDB:1U2W}.
STRAND 85 90 {ECO:0000244|PDB:1U2W}.
STRAND 96 100 {ECO:0000244|PDB:1U2W}.
HELIX 102 115 {ECO:0000244|PDB:1U2W}.
SEQUENCE 122 AA; 13779 MW; 7C60BBAFFEB91BC6 CRC64;
MKKKDTCEIF CYDEEKVNRI QGDLQTVDIS GVSQILKAIA DENRAKITYA LCQDEELCVC
DIANILGVTI ANASHHLRTL YKQGVVNFRK EGKLALYSLG DEHIRQIMMI ALAHKKEVKV
NV


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