CZCD_CUPMC
ID CZCD_CUPMC Reviewed; 316 AA.
AC P13512; Q58AM2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Metal cation efflux system protein CzcD;
DE AltName: Full=Cobalt-zinc-cadmium resistance protein CzcD;
GN Name=czcD; OrderedLocusNames=Rmet_5979;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OG Plasmid pMOL30.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2678100; DOI=10.1073/pnas.86.19.7351;
RA Nies D.H., Nies A., Chu L., Silver S.;
RT "Expression and nucleotide sequence of a plasmid-determined divalent cation
RT efflux system from Alcaligenes eutrophus.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7351-7355(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISCUSSION OF FUNCTION.
RX PubMed=9044283; DOI=10.1046/j.1365-2958.1997.d01-1866.x;
RA van der Lelie D., Schwuchow T., Schwidetzky T., Wuertz S., Baeyens W.,
RA Mergeay M., Nies D.H.;
RT "Two-component regulatory system involved in transcriptional control of
RT heavy-metal homoeostasis in Alcaligenes eutrophus.";
RL Mol. Microbiol. 23:493-503(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Monchy S., van der Lelie D., Vallaeys T., Taghavi S., Benotmane M.,
RA McCorkle S., Dunn J., Lapidus A., Mergeay M.;
RT "Sequence and features of the Ralstonia metallidurans CH34 heavy metals
RT plasmids pMOL28 and pMOL30.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=10559151; DOI=10.1128/jb.181.22.6876-6881.1999;
RA Anton A., Grosse C., Reissmann J., Pribyl T., Nies D.H.;
RT "CzcD is a heavy metal ion transporter involved in regulation of heavy
RT metal resistance in Ralstonia sp. strain CH34.";
RL J. Bacteriol. 181:6876-6881(1999).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF HIS-5; HIS-7; HIS-9;
RP GLU-31; HIS-49; MET-50; ASP-53; GLU-154; ASP-158; ASP-181; HIS-237;
RP HIS-251; HIS-280; CYS-290 AND HIS-298.
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=15516561; DOI=10.1128/jb.186.22.7499-7507.2004;
RA Anton A., Weltrowski A., Haney C.J., Franke S., Grass G., Rensing C.,
RA Nies D.H.;
RT "Characteristics of zinc transport by two bacterial cation diffusion
RT facilitators from Ralstonia metallidurans CH34 and Escherichia coli.";
RL J. Bacteriol. 186:7499-7507(2004).
CC -!- FUNCTION: Mediates a low-level metal ion resistance, probably by efflux
CC of cations from the cytoplasm into the periplasm. Also mediates
CC resistance to cobalt, cadmium and zinc via regulation of the Czc
CC system. May repress expression of the Czc system by an export of the
CC inducing cations. Binds and transports zinc. Can also bind cobalt,
CC copper and nickel. {ECO:0000269|PubMed:10559151,
CC ECO:0000269|PubMed:15516561}.
CC -!- ACTIVITY REGULATION: Efflux is inhibited by FCCP.
CC {ECO:0000269|PubMed:15516561}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:10559151}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10559151}.
CC -!- INDUCTION: Most highly expressed when the upstream czcCBA transcript is
CC not induced. {ECO:0000269|PubMed:9044283}.
CC -!- DISRUPTION PHENOTYPE: Mutant is impaired in metal sensing. Deletion
CC leads to partially constitutive expression of the Czc system due to an
CC increased transcription of the czcCBA genes.
CC {ECO:0000269|PubMed:10559151}.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
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DR EMBL; X98451; CAA67085.1; -; Genomic_DNA.
DR EMBL; X71400; CAI11245.1; -; Genomic_DNA.
DR EMBL; CP000354; ABF12838.1; -; Genomic_DNA.
DR RefSeq; WP_004635344.1; NC_007971.2.
DR RefSeq; YP_145596.1; NC_006466.1.
DR PDB; 6VD9; X-ray; 1.75 A; A/B/C/D=213-287.
DR PDBsum; 6VD9; -.
DR AlphaFoldDB; P13512; -.
DR SMR; P13512; -.
DR TCDB; 2.A.4.1.1; the cation diffusion facilitator (cdf) family.
DR EnsemblBacteria; ABF12838; ABF12838; Rmet_5979.
DR GeneID; 60820443; -.
DR KEGG; rme:Rmet_5979; -.
DR HOGENOM; CLU_013430_0_0_4; -.
DR OMA; GHEKMLH; -.
DR OrthoDB; 948593at2; -.
DR PRO; PR:P13512; -.
DR Proteomes; UP000002429; Plasmid pMOL30.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0010312; P:detoxification of zinc ion; IMP:CACAO.
DR GO; GO:0046686; P:response to cadmium ion; IEA:UniProtKB-KW.
DR GO; GO:0006829; P:zinc ion transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1510.10; -; 1.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR036837; Cation_efflux_CTD_sf.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF160240; SSF160240; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cadmium; Cadmium resistance; Cell inner membrane;
KW Cell membrane; Cobalt; Ion transport; Membrane; Plasmid;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Zinc;
KW Zinc transport.
FT CHAIN 1..316
FT /note="Metal cation efflux system protein CzcD"
FT /id="PRO_0000206105"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..46
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..114
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 5
FT /note="H->R: Decreases zinc resistance."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 7
FT /note="H->R: Lack of zinc resistance."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 9
FT /note="H->R: Decreases zinc resistance."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 31
FT /note="E->D: Decreases zinc resistance."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 31
FT /note="E->K: Lack of zinc resistance."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 49
FT /note="H->A: Lack of zinc resistance."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 50
FT /note="M->L: Hypersensitive to zinc."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 53
FT /note="D->A,E,N: Hypersensitive to zinc."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 154
FT /note="E->D,N: Lack of zinc resistance."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 158
FT /note="D->A,E: Lack of zinc resistance."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 181
FT /note="D->A: Decreases zinc resistance."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 181
FT /note="D->E,N: Hypersensitive to zinc."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 237
FT /note="H->R: Lack of zinc resistance."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 251
FT /note="H->A: Decreases zinc resistance."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 280
FT /note="H->A: Lack of zinc resistance."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 290
FT /note="C->S: Hypersensitive to zinc."
FT /evidence="ECO:0000269|PubMed:15516561"
FT MUTAGEN 298
FT /note="H->A: Lack of zinc resistance."
FT /evidence="ECO:0000269|PubMed:15516561"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:6VD9"
FT STRAND 230..240
FT /evidence="ECO:0007829|PDB:6VD9"
FT STRAND 246..254
FT /evidence="ECO:0007829|PDB:6VD9"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:6VD9"
FT HELIX 265..276
FT /evidence="ECO:0007829|PDB:6VD9"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:6VD9"
SQ SEQUENCE 316 AA; 33707 MW; 2977C1B4AEE9600F CRC64;
MGAGHSHDHP GGNERSLKIA LALTGTFLIA EVVGGVMTKS LALISDAAHM LTDTVALAIA
LAAIAIAKRP ADKKRTFGYY RFEILAAAFN ALLLFGVAIY ILYEAYLRLK SPPQIESTGM
FVVAVLGLII NLISMRMLSS GQSSSLNVKG AYLEVWSDLL GSVGVIAGAI IIRFTGWAWV
DSAIAVLIGL WVLPRTWILL KSSLNVLLEG VPDDVDLAEV EKQILATPGV KSFHDLHIWA
LTSGKASLTV HVVNDTAVNP EMEVLPELKQ MLADKFDITH VTIQFELAPC EQADAAQHFN
ASPALVGSKS LAAGGN
