ID   CZCS_RALME              Reviewed;         476 AA.
AC   Q44007; Q58AM0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   16-JUN-2009, entry version 76.
DE   RecName: Full=Sensor protein czcS;
DE            EC=2.7.13.3;
DE   Flags: Precursor;
GN   Name=czcS; OrderedLocusNames=Rmet_5977;
OS   Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839).
OG   Plasmid pMOL30.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=97197194; PubMed=9044283;
RX   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
RT   of 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
RT   metals plasmids pMOL28 and pMOL30.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Mergeay M., Benotmane M.A.,
RA   Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of plasmid pMOL30 of Ralstonia metallidurans
RT   CH34.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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: ATP + protein L-histidine = ADP + protein N-
CC       phospho-L-histidine.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane
CC       protein (Potential).
CC   -!- INDUCTION: By cadmium, lead, and zinc.
CC   -!- SIMILARITY: Contains 1 HAMP domain.
CC   -!- SIMILARITY: Contains 1 histidine kinase domain.
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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; YP_145598.1; -.
DR   RefSeq; YP_581786.1; -.
DR   GeneID; 3170507; -.
DR   GeneID; 4036512; -.
DR   GenomeReviews; CP000354_GR; Rmet_5977.
DR   KEGG; rme:Rmet_5977; -.
DR   HOGENOM; Q44007; -.
DR   OMA; Q44007; DSNIEEC.
DR   BioCyc; RMET266264:RMET_5977-MON; -.
DR   BRENDA; 2.7.13.3; 1263.
DR   GO; GO:0016021; C:integral to 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:0046870; F:cadmium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:two-component sensor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0018106; P:peptidyl-histidine phosphorylation; IEA:InterPro.
DR   GO; GO:0007600; P:sensory perception; IEA:InterPro.
DR   GO; GO:0000160; P:two-component signal transduction system (p...; IEA:UniProtKB-KW.
DR   InterPro; IPR003594; ATP_bd_ATPase.
DR   InterPro; IPR003660; HAMP_linker_domain.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR006290; Sig_transdc_His_kin_metal-sen.
DR   InterPro; IPR003661; Sig_transdc_His_kin_sub1_dim/P.
DR   InterPro; IPR005467; Sig_transdc_His_kinase_core.
DR   Gene3D; G3DSA:3.30.565.10; ATP_bd_ATPase; 1.
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   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;
KW   Complete proteome; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Plasmid; Signal; Transferase; Transmembrane;
KW   Two-component regulatory system; Zinc.
FT   SIGNAL        1     35       Potential.
FT   CHAIN        36    476       Sensor protein czcS.
FT                                /FTId=PRO_0000074746.
FT   TOPO_DOM     37    158       Periplasmic (Potential).
FT   TRANSMEM    159    179       Potential.
FT   TOPO_DOM    180    476       Cytoplasmic (Potential).
FT   DOMAIN      181    234       HAMP.
FT   DOMAIN      242    455       Histidine kinase.
FT   MOD_RES     245    245       Phosphohistidine; by autocatalysis (By
FT                                similarity).
FT   CONFLICT    377    379       EAA -> DR (in Ref. 1; CAA67087).
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
//