ZRAS_SALTY
ID ZRAS_SALTY Reviewed; 465 AA.
AC P37461; Q9L9H9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Sensor protein ZraS;
DE EC=2.7.13.3;
GN Name=zraS; Synonyms=hydH; OrderedLocusNames=STM4173; ORFNames=STMF1.26;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 258-465.
RX PubMed=1756170; DOI=10.1016/0167-4781(91)90224-a;
RA Chopra A.K., Peterson J.W., Prasad R.;
RT "Cloning and sequence analysis of hydrogenase regulatory genes (hydHG) from
RT Salmonella typhimurium.";
RL Biochim. Biophys. Acta 1129:115-118(1991).
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 -!- CAUTION: Was originally thought to be involved in the regulation of the
CC labile hydrogenase activity. {ECO:0000305|PubMed:1756170}.
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DR EMBL; AF170176; AAF33505.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23001.1; -; Genomic_DNA.
DR EMBL; M64988; AAA27148.1; -; mRNA.
DR PIR; S19605; S19605.
DR RefSeq; NP_463042.1; NC_003197.2.
DR RefSeq; WP_001526924.1; NC_003197.2.
DR AlphaFoldDB; P37461; -.
DR SMR; P37461; -.
DR STRING; 99287.STM4173; -.
DR PaxDb; P37461; -.
DR EnsemblBacteria; AAL23001; AAL23001; STM4173.
DR GeneID; 1255699; -.
DR KEGG; stm:STM4173; -.
DR PATRIC; fig|99287.12.peg.4387; -.
DR HOGENOM; CLU_000445_89_29_6; -.
DR OMA; QAIFTPY; -.
DR PhylomeDB; P37461; -.
DR BioCyc; SENT99287:STM4173-MON; -.
DR BRENDA; 2.7.13.3; 5542.
DR Proteomes; UP000001014; 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 2: Evidence at transcript level;
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..465
FT /note="Sensor protein ZraS"
FT /id="PRO_0000074913"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
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; 51254 MW; 615F8346224FB3F6 CRC64;
MSFIRLHKDA AATWLSRLLP AAIFILVGLF SIMVIRDYGR ESAAARQTLL EKGNVLIRAL
ESGTRVGMGM RMHHAQQQTL LEEMAGQPGV LWFAVTDAQG VIITHSNPGM VGKSLYSPSE
MHQLNPGPQE RWRRVDVAAN GETVPALEIY RQFQPLFGMR GHGMRGHGMA RSANDDEPAK
QTIFIAFDAS ELAATQAREW RNTLIVLSAL AAVLLATLLA FFWHQRYQRS HRELLDAMKR
KEKLVAMGHL AAGVAHEIRN PLSSIKGLAK YFAERTPAGG ESHELAQVMA KEADRLNRVV
SELLELVKPA HLTLQTVNLN DIITHSLNLV SQDAQSREIQ LRFTANETLK RIQADPDRLT
QVLLNLYLNA IHAIGRQGTI SVEAKESGTD RVIITVTDSG KGIAPDQLEA IFTPYFTTKA
DGTGLGLAVV QNIIEQHGGA IKVKSIEGKG AVFTIWLPVI ARQQD