CZCA_CUPMC
ID CZCA_CUPMC Reviewed; 1063 AA.
AC P13511; P94142; Q58AM3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 3.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Cobalt-zinc-cadmium resistance protein CzcA;
DE AltName: Full=Cation efflux system protein CzcA;
GN Name=czcA; OrderedLocusNames=Rmet_5980;
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 TO 918 AND 959-960.
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: Has a low cation transport activity for cobalt, it is
CC essential for the expression of cobalt, zinc, and cadmium resistance.
CC CzcA and CzcB together would act in zinc efflux nearly as effectively
CC as the complete CZC efflux system (CzcABC).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
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 resistance-nodulation-cell division (RND)
CC (TC 2.A.6) family. {ECO:0000305}.
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DR EMBL; X98451; CAA67084.1; -; Genomic_DNA.
DR EMBL; X71400; CAI11244.1; -; Genomic_DNA.
DR EMBL; CP000354; ABF12839.1; -; Genomic_DNA.
DR PIR; A33830; A33830.
DR RefSeq; WP_011229347.1; NC_007971.2.
DR RefSeq; YP_145595.1; NC_006466.1.
DR AlphaFoldDB; P13511; -.
DR SMR; P13511; -.
DR TCDB; 2.A.6.1.2; the resistance-nodulation-cell division (rnd) superfamily.
DR EnsemblBacteria; ABF12839; ABF12839; Rmet_5980.
DR KEGG; rme:Rmet_5980; -.
DR HOGENOM; CLU_002755_1_2_4; -.
DR OMA; PMALTFI; -.
DR OrthoDB; 91817at2; -.
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:0046686; P:response to cadmium ion; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2090.10; -; 2.
DR InterPro; IPR027463; AcrB_DN_DC_subdom.
DR InterPro; IPR001036; Acrflvin-R.
DR InterPro; IPR004763; CzcA/CusA/SilA/NccA/HelA/CnrA.
DR PANTHER; PTHR32063; PTHR32063; 1.
DR Pfam; PF00873; ACR_tran; 1.
DR PRINTS; PR00702; ACRIFLAVINRP.
DR SUPFAM; SSF82714; SSF82714; 2.
DR TIGRFAMs; TIGR00914; 2A0601; 1.
PE 1: Evidence at protein level;
KW Cadmium resistance; Cell inner membrane; Cell membrane; Cobalt; Membrane;
KW Plasmid; Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Zinc.
FT CHAIN 1..1063
FT /note="Cobalt-zinc-cadmium resistance protein CzcA"
FT /id="PRO_0000161818"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 883..903
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 906..926
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 937..957
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 981..1001
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1013..1033
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1040..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 918
FT /note="T -> I (in Ref. 1; CAA67084)"
FT /evidence="ECO:0000305"
FT CONFLICT 959..960
FT /note="SL -> LV (in Ref. 1; CAA67084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1063 AA; 115644 MW; 47AF0AA18E0D4D2E CRC64;
MFERIISFAI QQRWLVLLAV FGMAGLGIFS YNRLPIDAVP DITNVQVQVN TSAPGYSPLE
TEQRATYPIE VVMAGLPGLE QTRSLSRYGL SQVTVIFKDG TDVYFARQLV NQRIQEAKDN
LPEGVVPAMG PISTGLGEIY LWTVEAEEGA RKADGTAYTP TDLREIQDWV VRPQLRNVPG
VTEINTIGGF NKQYLVAPSL ERLASYGLTL TDVVNALNKN NDNVGAGYIE RRGEQYLVRA
PGQVASEDDI RNIIVGTAQG QPIRIRDIGD VEIGKELRTG AATENGKEVV LGTVFMLIGE
NSRAVSKAVD EKVASINRTM PEGVKIVTVY DRTRLVDKAI ATVKKNLLEG AVLVIVILFL
FLGNIRAALI TATIIPLAML FTFTGMVNYK ISANLMSLGA LDFGIIIDGA VVIVENCVRR
LAHAQEHHGR PLTRSERFHE VFAAAKEARR PLIFGQLIIM IVYLPIFALT GVEGKMFHPM
AFTVVLALLG AMILSVTFVP AAVALFIGER VAEKENRLML WAKRRYEPLL EKSLANTAVV
LTFAAVSIVL CVAIAARLGS EFIPNLNEGD IAIQALRIPG TSLSQSVEMQ KTIETTLKAK
FPEIERVFAR TGTAEIASDL MPPNISDGYI MLKPEKDWPE PKKTHAELLS AIQEEAGKIP
GNNYEFSQPI QLRFNELISG VRSDVAVKIF GDDNNVLSET AKKVSAVLQG IPGAQEVKVE
QTTGLPMLTV KIDREKAARY GLNMSDVQDA VATGVGGRDS GTFFQGDRRF DIVVRLPEAV
RGEVEALRRL PIPLPKGVDA RTTFIPLSEV ATLEMAPGPN QISRENGKRR IVISANVRGR
DIGSFVPEAE AAIQSQVKIP AGYWMTWGGT FEQLQSATTR LQVVVPVALL LVFVLLFAMF
NNIKDGLLVF TGIPFALTGG ILALWIRGIP MSITAAVGFI ALCGVAVLNG LVMLSFIRSL
REEGHSLDSA VRVGALTRLR PVLMTALVAS LGFVPMAIAT GTGAEVQRPL ATVVIGGILS
STALTLLVLP VLYRLAHRKD EDAEDTREPV TQTHQPDQGR QPA
