ID   CUTS_STRCO              Reviewed;         414 AA.
AC   P0A4I7; Q03757;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Sensor protein CutS;
DE            EC=2.7.13.3;
GN   Name=cutS; OrderedLocusNames=SCO5863; ORFNames=SC2E9.04;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Member of the two-component regulatory system CutS/CutR,
CC       involved in the regulation of copper metabolism.
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 membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AL939125; CAA16472.1; -; Genomic_DNA.
DR   PIR; T34815; T34815.
DR   RefSeq; NP_629985.1; NC_003888.3.
DR   RefSeq; WP_003973157.1; NZ_VNID01000007.1.
DR   AlphaFoldDB; P0A4I7; -.
DR   SMR; P0A4I7; -.
DR   STRING; 100226.SCO5863; -.
DR   GeneID; 1101305; -.
DR   KEGG; sco:SCO5863; -.
DR   PATRIC; fig|100226.15.peg.5962; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_89_3_11; -.
DR   InParanoid; P0A4I7; -.
DR   OMA; FPWLRPT; -.
DR   PhylomeDB; P0A4I7; -.
DR   BRENDA; 2.7.13.3; 5998.
DR   Proteomes; UP000001973; Chromosome.
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; 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   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..414
FT                   /note="Sensor protein CutS"
FT                   /id="PRO_0000074744"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          142..194
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          202..414
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         205
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   414 AA;  44496 MW;  B1CBC2DFBD0ABB4D CRC64;
     MATTPAPPGA PPKPTWDPRS ATPLPWLRPT IRIRLTLLYG GMFLIAGILL LSIIYLLAAQ
     AVRTGNEPLY KIVDFTDLKV SSSTCPVVDN GGLSLSDFNA AISDCMDHQR KVALDNLLSR
     SLLALLGLAV IAFAFGYAMA GRVLSPLGRI TRTARAVAGS DLSRRIELDG PDDELKELAD
     TFDDMLERLQ RAFTAQQRFV GNASHELRTP LAINRTLLEV HLSDPGAPVE LQQLGKTLLA
     TNERSELLVE GLLLLARSDN QIVERKPVDL AEVAGQAIDQ VHAEAESKGV EVRGTREAAV
     VQGNGVLLER IALNLVQNAV RYNVAGQGWV EVATAVENGQ AVLVVTNTGP VVPAYEVDNL
     FEPFRRLRTE RTGSDKGVGL GLSIARSVAR AHGGHISAQP REGGGLVMRV TLPV