ID   COPS_PSEUB              Reviewed;         487 AA.
AC   Q02541;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Sensor protein CopS;
DE            EC=2.7.13.3;
GN   Name=copS;
OS   Pseudomonas syringae pv. tomato.
OG   Plasmid pPT23D.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8449873; DOI=10.1128/jb.175.6.1656-1664.1993;
RA   Mills S.D., Jasalavich C.A., Cooksey D.A.;
RT   "A two-component regulatory system required for copper-inducible expression
RT   of the copper resistance operon of Pseudomonas syringae.";
RL   J. Bacteriol. 175:1656-1664(1993).
CC   -!- FUNCTION: Member of the two-component regulatory system CopS/CopR.
CC       Involved in the activation of copper resistance gene operon copABCD.
CC       Specifically recognizes or transduces a signal only in response to
CC       copper. This would lead to phosphorylation of CopR in the cytoplasm.
CC       CopS/CopR may also regulate chromosomally encoded genes. May also be
CC       involved in basic 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 inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
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DR   EMBL; L05176; AAA25804.1; -; Genomic_DNA.
DR   PIR; C47080; C47080.
DR   AlphaFoldDB; Q02541; -.
DR   SMR; Q02541; -.
DR   BRENDA; 2.7.13.3; 5193.
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   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
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   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Copper; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Plasmid; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..487
FT                   /note="Sensor protein CopS"
FT                   /id="PRO_0000074737"
FT   TOPO_DOM        1..9
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..159
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..487
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"
SQ   SEQUENCE   487 AA;  53457 MW;  A9D678AACBC077FD CRC64;
     MKPGSLTLRL SLLFVVAVAA VLIIVGVAFN ELSRHHFRAL DAQALGEKLE AITQIAKESG
     ANPELLKARW HTLLGAHPDL SAVFLKTDGT PFFAEPPQSA VPSLAQATQR DGVWEWEKEG
     RMFRALTASV SLPTASPPLT AWLVLDVTTH MHFFAMLERW FWGVLLASTV LSAALGWLVA
     KNGLRPVARV TQTAASMSAG SLKERIPLEP VPDELRALIT AFNSMLGRLD DSFMRLSNFS
     ADIAHELRTP ISNLRTHTEV ILAKKRAPEV YEENLSSNLE ELNRLSGIID GMLFLAKSDN
     GLIVPEAVEL DLRTVISKLF GYYEFLAEDK GIQLQASGNA SIFADSVMID RVVSNLLSNA
     LRYTSSGETI KVSIHDHGGR VELRLENPGP EIVPQHLDRI FDRFYRVDPA RREGRECGAG
     ASDCPVLDAS AWRHYLVYIP RGPNDLHPHL HAIACPTNLT CRPDSLGTAK PGHTRLGEHE
     TGCHCAG