ID   CZCB_CUPMC              Reviewed;         520 AA.
AC   P13510; Q58AM4;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   25-MAY-2022, entry version 134.
DE   RecName: Full=Cobalt-zinc-cadmium resistance protein CzcB;
DE   AltName: Full=Cation efflux system protein CzcB;
GN   Name=czcB; OrderedLocusNames=Rmet_5981;
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   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   SEQUENCE REVISION.
RA   van der Lelie D., Schwuchow T., Wuertz S., Schwidetzky U., Baeyens W.,
RA   Scheel P.O., Nies D.H.;
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
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   CHARACTERIZATION, INDUCTION, AND POSSIBLE MODE OF ACTION.
RX   PubMed=7766206; DOI=10.1007/bf01569896;
RA   Diels L., Dong Q., van der Lelie D., Baeyens W., Mergeay M.;
RT   "The czc operon of Alcaligenes eutrophus CH34: from resistance mechanism to
RT   the removal of heavy metals.";
RL   J. Ind. Microbiol. 14:142-153(1995).
CC   -!- FUNCTION: CzcA and CzcB together would act in zinc efflux nearly as
CC       effectively as the complete czc efflux system (CzcABC). The CzcB
CC       protein is thought to funnel zinc cations to the CzcA transport
CC       protein.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}. Note=May be anchored in the inner
CC       membrane, cross the periplasm and contact the outer membrane as
CC       proposed for membrane fusion proteins.
CC   -!- INDUCTION: By zinc, cadmium and cobalt (zinc being the best and cobalt
CC       being the worst inducer). {ECO:0000269|PubMed:7766206}.
CC   -!- BIOTECHNOLOGY: In the presence of 2 mM Cd(2+) or 4-10 mM Zn(2+) up to
CC       99% of the metal is removed from the culture supernatant and is
CC       sequestered via bioprecipitation. Additionally Cu(2+), Co(2+), Ni(2+),
CC       Pb(2+), Y(3+) and Ge(4+) can also be removed from culture supernatants,
CC       although it is not clear which efflux system is responsible for all
CC       these substrates (PubMed:7766206). {ECO:0000269|PubMed:7766206}.
CC   -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC       family. {ECO:0000305}.
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DR   EMBL; X98451; CAA67083.1; -; Genomic_DNA.
DR   EMBL; X71400; CAI11243.1; -; Genomic_DNA.
DR   EMBL; CP000354; ABF12840.1; -; Genomic_DNA.
DR   PIR; B33830; B33830.
DR   RefSeq; WP_004635340.1; NC_007971.2.
DR   RefSeq; YP_145594.1; NC_006466.1.
DR   AlphaFoldDB; P13510; -.
DR   SMR; P13510; -.
DR   TCDB; 2.A.6.1.2; the resistance-nodulation-cell division (rnd) superfamily.
DR   EnsemblBacteria; ABF12840; ABF12840; Rmet_5981.
DR   GeneID; 60820445; -.
DR   KEGG; rme:Rmet_5981; -.
DR   HOGENOM; CLU_018816_13_0_4; -.
DR   OMA; VIPKREY; -.
DR   OrthoDB; 1174564at2; -.
DR   PRO; PR:P13510; -.
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:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046686; P:response to cadmium ion; IEA:UniProtKB-KW.
DR   InterPro; IPR005695; Co/Zn/Cd_resistance_CzcB.
DR   InterPro; IPR043602; CusB_dom_1.
DR   InterPro; IPR032317; HlyD_D23.
DR   InterPro; IPR006143; RND_pump_MFP.
DR   Pfam; PF00529; CusB_dom_1; 1.
DR   Pfam; PF16576; HlyD_D23; 1.
DR   TIGRFAMs; TIGR00999; 8a0102; 1.
DR   TIGRFAMs; TIGR01730; RND_mfp; 1.
PE   1: Evidence at protein level;
KW   Cadmium resistance; Cell inner membrane; Cell membrane; Cobalt;
KW   Coiled coil; Membrane; Plasmid; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Zinc.
FT   CHAIN           1..520
FT                   /note="Cobalt-zinc-cadmium resistance protein CzcB"
FT                   /id="PRO_0000201867"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          28..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          286..320
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        36..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        338
FT                   /note="D -> A (in Ref. 1; CAA67083)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   520 AA;  54631 MW;  0E4A460A887F79A4 CRC64;
     MAISNKQKAA IAAIVLVGGV ATGGVLLSGR SAPEEQGGHS ESKGHGDTEH HGKQAAEADH
     KDDKSHGDGE HHEVKKGPNG GALFSRDGYD VEIGTAESKG EARIRLWVSK SGKAVANGVA
     ATGQLVRATG ESQALKFVVS GDALESQQPV AEPHVFDVTA NVTLPGSSSP LAVRLSKEEG
     KIELTADQLA KTGVVVQTAG SAKVQAGVQF PGEIRFNEDK TAHVVPRLAG VVESVPANIG
     QQVKKGQVLA VIASTGLSDQ RSELLAAQKR LDLARVTYDR EKKLWEQKIS AEQDYLSARN
     ALQEAQISVQ NAQQKLTAIG ASNSSTALNR YELRAPFDGM IVEKHISLGE AVADNANVFT
     LSDLSSVWAE FVVSAKDVER VRIGEKASIN SASSDVKADG TVSYVGSLLG EQTRTAKARV
     TLTNPQMAWR PGLFVTVDVF GADVEVPVAV KTEAVQDVNG ESVVFVAVQG GFVPQPVKVG
     RTNGKVIEIV EGLKPGARYA AANSFVLKAE LGKSSAEHGH