ZRAR_SALTI
ID ZRAR_SALTI Reviewed; 441 AA.
AC Q8Z333;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Transcriptional regulatory protein ZraR;
GN Name=zraR; Synonyms=hydG; OrderedLocusNames=STY3711, t3457;
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. When
CC activated by ZraS it acts in conjunction with sigma-54 to regulate the
CC expression of zraP. Positively autoregulates the expression of the
CC zraSR operon (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by ZraS. {ECO:0000250}.
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DR EMBL; AL513382; CAD09470.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70973.1; -; Genomic_DNA.
DR RefSeq; NP_457900.1; NC_003198.1.
DR RefSeq; WP_000617932.1; NZ_WSUR01000043.1.
DR AlphaFoldDB; Q8Z333; -.
DR SMR; Q8Z333; -.
DR STRING; 220341.16504587; -.
DR EnsemblBacteria; AAO70973; AAO70973; t3457.
DR KEGG; stt:t3457; -.
DR KEGG; sty:STY3711; -.
DR PATRIC; fig|220341.7.peg.3783; -.
DR eggNOG; COG2204; Bacteria.
DR HOGENOM; CLU_000445_0_6_6; -.
DR OMA; MPISMQV; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR PRINTS; PR01590; HTHFIS.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 3: Inferred from homology;
KW Activator; ATP-binding; Cytoplasm; DNA-binding; Nucleotide-binding;
KW Phosphoprotein; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..441
FT /note="Transcriptional regulatory protein ZraR"
FT /id="PRO_0000081282"
FT DOMAIN 7..121
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 141..370
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 421..440
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 232..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 441 AA; 48499 MW; A071FB6466113204 CRC64;
MIRGKIDILV VDDDVSHCTI LQALLRGWGY NVALAYSGHD ALAQVREKVF DLVLCDVRMA
EMDGIATLKE IKALNPAIPI LIMTAFSSVE TAVEALKAGA LDYLIKPLDF DRLQETLEKA
LAHTRETGAE LPSASAAQFG MIGSSPAMQH LLNEIAMVAP SDATVLIHGD SGTGKELVAR
ALHACSARSD KPLVTLNCAA LNESLLESEL FGHEKGAFTG ADKRREGRFV EADGGTLFLD
EIGDISPLMQ VRLLRAIQER EVQRVGSNQT ISVDVWLIAA THRDLAEEVS AGRFRQDLYY
RLNVVAIEMP SLRQRREDIP LLADHFLRRF AERNRKAVKG FTPQAMDLLI HYDWPGNIRE
LENAIERAVV LLTGEYISER ELPLAIAATP IKAENSAEIQ PLVDVEKEVI LAALEKTGGN
KTEAARQLGI TRKTLLAKLS R
