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 27-MAR-2024, entry version 159.
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; Pseudomonadota; 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 GeneID; 70691411; -.
DR KEGG; rme:Rmet_5977; -.
DR HOGENOM; CLU_000445_89_6_4; -.
DR BRENDA; 2.7.13.3; 231.
DR Proteomes; UP000002429; Plasmid pMOL30.
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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR048590; CusS-like_sensor.
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 NCBIfam; TIGR01386; cztS_silS_copS; 1.
DR PANTHER; PTHR45436:SF15; SENSOR HISTIDINE KINASE CRDS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF21085; CusS; 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 SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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
//
