ZRAS_SALTI
ID ZRAS_SALTI Reviewed; 465 AA.
AC Q8Z332;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Sensor protein ZraS;
DE EC=2.7.13.3;
GN Name=zraS; Synonyms=hydH; OrderedLocusNames=STY3712, t3458;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD09471.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70974.1; -; Genomic_DNA.
DR RefSeq; NP_457901.1; NC_003198.1.
DR RefSeq; WP_001772857.1; NZ_WSUR01000043.1.
DR AlphaFoldDB; Q8Z332; -.
DR SMR; Q8Z332; -.
DR STRING; 220341.16504588; -.
DR EnsemblBacteria; AAO70974; AAO70974; t3458.
DR KEGG; stt:t3458; -.
DR KEGG; sty:STY3712; -.
DR PATRIC; fig|220341.7.peg.3784; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_89_29_6; -.
DR OMA; QAIFTPY; -.
DR BRENDA; 2.7.13.3; 5557.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system; Zinc.
FT CHAIN 1..465
FT /note="Sensor protein ZraS"
FT /id="PRO_0000074912"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 253..461
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 256
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 465 AA; 51241 MW; FAFEBAA7600855D7 CRC64;
MSFIRLHKDA AAMWLSRLLP AAIFILVGLF SIMVIRDYGR ESAAARQTLL EKGNVLIRAL
ESGTRVGMGM RMHHAQQQTL LEEMAGQPGV LWFAVTDAQG VIITHSNPGM VGKSLYSPSE
MHQLNPGPQE CWRRVDVAAN GETVPALEIY RQFQPLFGMR GHGMRGHGMA RSANDDEPAK
QTIFIAFDAS ELAATQAREW RNTLIVLSAL AAVLLATLLA FFWYQRYQRS HRELLDAMKR
KEKLVAMGHL AAGVAHEIRN PLSSIKGLAK YFAERTPAGG ESHELAQVMA KEADRLNRVV
SELLELVKPA HLTLQAVNLN DIITHSLNLV SQDAQSREIQ LRFTANETLK RIQADPDRLT
QVLLNLYLNA IHAIGRQGTI TVEAKESGTD RVIITVTDSG KGIAPDQLEA IFTPYFTTKA
DGTGLGLAVV QNIIEQHGGA IKVKSIEGKG AVFTIWLPVI ARQQD