ID   ZRAS_ECO57              Reviewed;         458 AA.
AC   Q8X614;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Sensor protein ZraS;
DE            EC=2.7.13.3;
GN   Name=zraS; Synonyms=hydH; OrderedLocusNames=Z5579, ECs4926;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(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}.
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DR   EMBL; AE005174; AAG59200.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38349.1; -; Genomic_DNA.
DR   PIR; D86092; D86092.
DR   PIR; F91244; F91244.
DR   RefSeq; NP_312953.1; NC_002695.1.
DR   RefSeq; WP_001211936.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8X614; -.
DR   SMR; Q8X614; -.
DR   STRING; 155864.EDL933_5335; -.
DR   EnsemblBacteria; AAG59200; AAG59200; Z5579.
DR   EnsemblBacteria; BAB38349; BAB38349; ECs_4926.
DR   GeneID; 916224; -.
DR   KEGG; ece:Z5579; -.
DR   KEGG; ecs:ECs_4926; -.
DR   PATRIC; fig|386585.9.peg.5152; -.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_89_29_6; -.
DR   OMA; QAIFTPY; -.
DR   BRENDA; 2.7.13.3; 2026.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; 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; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix; Two-component regulatory system; Zinc.
FT   CHAIN           1..458
FT                   /note="Sensor protein ZraS"
FT                   /id="PRO_0000074910"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          244..451
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         247
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   458 AA;  50557 MW;  8B5526C4A1870F80 CRC64;
     MRFMQRSKDS LAKWLSAILP VVIVGLVGLF AVTVIRDYGR ETAAARQTLL EKGSVLIRAL
     ESGSRVGMGM RMHHAQQQAL LEEMAGQPGV RWFAVTDEQG TIVMHSNSGM VGKQLYSPQE
     MQQLHPGDEE VWRRIDSADG EPVLEIYRQF QPMFAAGMHR MRHMQQYAAT PQAIFIAFDA
     SNIVSAEDRE QRNTLIILFA LATVLLASVL SFFWYRRYLR SRQLLQDEMK RKEKLVALGH
     LAAGVAHEIR NPLSSIKGLA KYFAERAPAG GEAHQLAQVM AKEADRLNRV VSELLELVKP
     THLALQAVDL NTLINHSLQL VSQDANCREI QLRFTANDTL PEIQADPDRL TQVLLNLYLN
     AIQAIGQHGV ISVTASESGA GVKISVTDSG KGIAADQLEA IFTPYFTTKA EGTGLGLAVV
     HNIVEQHGGT IQVASLEGKG ARFTLWLPVN ITRKDPQG