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CZCS_CUPMC
ID   CZCS_CUPMC              Reviewed;         476 AA.
AC   Q44007; Q58AM0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   25-MAY-2022, entry version 150.
DE   RecName: Full=Sensor protein CzcS;
DE            EC=2.7.13.3;
DE   Flags: Precursor;
GN   Name=czcS; OrderedLocusNames=Rmet_5977;
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=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   [2]
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   [3]
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).
CC   -!- FUNCTION: Member of the two-component regulatory system CzcS/CzcR
CC       involved in the control of cobalt, zinc and cadmium homeostasis.
CC       Probably activates CzcR by phosphorylation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- INDUCTION: By cadmium, lead, and zinc.
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DR   EMBL; X71400; CAI11247.1; -; Genomic_DNA.
DR   EMBL; X98451; CAA67087.1; -; Genomic_DNA.
DR   EMBL; CP000354; ABF12836.1; -; Genomic_DNA.
DR   RefSeq; WP_011229349.1; NC_007971.2.
DR   RefSeq; YP_145598.1; NC_006466.1.
DR   AlphaFoldDB; Q44007; -.
DR   SMR; Q44007; -.
DR   EnsemblBacteria; ABF12836; ABF12836; Rmet_5977.
DR   GeneID; 60820441; -.
DR   KEGG; rme:Rmet_5977; -.
DR   HOGENOM; CLU_000445_89_6_4; -.
DR   OMA; HDEVQDV; -.
DR   BRENDA; 2.7.13.3; 231.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR006290; CztS_silS_copS.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR01386; cztS_silS_copS; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cadmium; Cell inner membrane; Cell membrane; Cobalt; Kinase;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Plasmid; Reference proteome;
KW   Signal; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system; Zinc.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..476
FT                   /note="Sensor protein CzcS"
FT                   /id="PRO_0000074746"
FT   TOPO_DOM        37..158
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        180..476
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          181..234
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          242..455
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         245
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   CONFLICT        377..379
FT                   /note="EAA -> DR (in Ref. 1; CAA67087)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   476 AA;  52010 MW;  657329F4162C6326 CRC64;
     MRPGTSITPL SLTRRLGLFF ALVLSIALAS MGAFAYYSLA AQLEARDDEV VKGKLEQVEH
     FLREVDGVQG VPAAQHRFDD LVRGYSDLIV RVTALDGRLL FRTGNDALLE GTDQAAVTGK
     SSLMFQSADA VLGRDGTRAT VFVAKSGEDR KQVTARFRTT LVLGTTVGVI LTALVGAAIT
     RRELEPAHVL IKQINRISVE RLSYRVDMPP KPTEVRDIAS AFNAMLQRLE DGYQKLSRFS
     ADLAHDLRTP LNNLIGHAEV ALSRDRTGPE YVALVEESLV EYQRLARMID AMLFLARADS
     ANVALELTEL QLNAELRKLS AYFSVLAEER SVVIRVSGDA TLVADAILFQ RAINNVLSNA
     VRHAWPNSMI DLVVRREAAH CCIDITNVGD PIPERELSLI FDRFFRGDRA RSNSSQSTGL
     GLAIVLSIME LHGGDASAVS GLDGKTRFTL RFPLNGAEAS ARVSVGRPSQ DRPVVG
 
 
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