ZRAR_KLEOX
ID ZRAR_KLEOX Reviewed; 443 AA.
AC Q9APD9;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Transcriptional regulatory protein ZraR;
GN Name=zraR; Synonyms=hydG;
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. 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:0000305}.
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DR EMBL; AF305914; AAG59807.1; -; Genomic_DNA.
DR RefSeq; WP_004870527.1; NZ_LR607357.1.
DR AlphaFoldDB; Q9APD9; -.
DR SMR; Q9APD9; -.
DR PATRIC; fig|571.110.peg.238; -.
DR OrthoDB; 123059at2; -.
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..443
FT /note="Transcriptional regulatory protein ZraR"
FT /id="PRO_0000081281"
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 423..442
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 443 AA; 48900 MW; EEC0A6C8D375A4DF CRC64;
MSGEQVDILV VDDDISHCTI LQALLRGWGY RVALANNGLQ ALEKVREKVF DLVLCDIRMA
EMDGIETLKE IKTFNPSIPV LIMTAYSSVD TAVEALKSGA LDYLIKPLDF DKLQLTLSEA
LAHTRLSESP VTETPAAQFG MVGDSPAMRA LLNNITLVAP SDATVLIHGE SGTGKELVAR
ALHASSARSR RPLVILNCAA LNESLLESEL FGHEKGAFTG ADKRREGRFV EADGGTLFLD
EIGDISPLMQ VRLLRAIQER EVQRVGSNQT LSVDVRLIAA THRDLAEEVS AGRFRQDLYY
RLNVVTIDMP PLRHRREDIP PLARYFLQRY AERNRKAVQG FTPQAMDLLI HYAWPGNIRE
LENAVERAVV LLTGEYISER ELPLAITGTP VADAPHGDDS IQPLVEVEKE AILAALERTG
GNKTEAARRL GITRKTLLAK LSR