ID   ZRAS_KLEOX              Reviewed;         462 AA.
AC   Q9APE0;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Sensor protein ZraS;
DE            EC=2.7.13.3;
GN   Name=zraS; Synonyms=hydH;
OS   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M5a1;
RX   PubMed=11243806; DOI=10.1006/jmbi.2000.4451;
RA   Leonhartsberger S., Huber A., Lottspeich F., Boeck A.;
RT   "The hydH/G genes from Escherichia coli code for a zinc and lead responsive
RT   two-component regulatory system.";
RL   J. Mol. Biol. 307:93-105(2001).
CC   -!- FUNCTION: Member of the two-component regulatory system ZraS/ZraR. May
CC       function as a membrane-associated protein kinase that phosphorylates
CC       ZraR in response to high concentrations of zinc or lead in the medium
CC       (By similarity). {ECO:0000250}.
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:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF305914; AAG59806.1; -; Genomic_DNA.
DR   RefSeq; WP_004870525.1; NZ_QDDU01000035.1.
DR   AlphaFoldDB; Q9APE0; -.
DR   SMR; Q9APE0; -.
DR   STRING; 571.MC52_09515; -.
DR   PATRIC; fig|571.110.peg.237; -.
DR   eggNOG; COG4191; Bacteria.
DR   OrthoDB; 1755994at2; -.
DR   BRENDA; 2.7.13.3; 2811.
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; 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; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF103190; SSF103190; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system; Zinc.
FT   CHAIN           1..462
FT                   /note="Sensor protein ZraS"
FT                   /id="PRO_0000074911"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          247..455
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         250
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   462 AA;  51201 MW;  738FDED1BC27214B CRC64;
     MNVMRLSKDS VAVGLSWLLT GLILLLVCLF SALIVRDYGR ENEAARQTIQ EKGSVLIRAL
     ESGTRVGMGM RMHHSQLQTL LEEMAWQPGV LWFAVTDENG KIIAHSDPRR VGESLYPAST
     LRELNIGSEE RWRRLEQPEP ALEIYRQFRP LNGGGHHMRM MMRRESADLR NQAPQVIFIA
     FDTRELDADH ARGLRNMVIM LCAAGVVMAA TVLAQFWFRR YQRSRKQLQE ATARKEKLVA
     LGHLAAGVAH EIRNPLSSIK GLAKYFAERT PADGEAHQLA LVMAREADRL NRVVSELLEL
     VRPAHLKYQS VDLNEVITHS LQLVSQDAAS RAISLTFTAQ PALCRIQADP DRLKQVLLNL
     YLNAVHAIGR EGVITVAVRE CGDGRVKVSV ADSGKGMTAE QLQAIFTPYF STKADGTGLG
     LAVVQNIVEQ HGGTIDAESA PGKGALFTFY LPVNGQQKDE QG