ZRAR_ECOLI
ID ZRAR_ECOLI Reviewed; 441 AA.
AC P14375; Q2M8U1;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Transcriptional regulatory protein ZraR;
GN Name=zraR; Synonyms=hydG; OrderedLocusNames=b4004, JW3968;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2666400; DOI=10.1128/jb.171.8.4448-4456.1989;
RA Stoker K., Reijnders W.N.M., Oltmann L.F., Stouthamer A.H.;
RT "Initial cloning and sequencing of hydHG, an operon homologous to ntrBC and
RT regulating the labile hydrogenase activity in Escherichia coli K-12.";
RL J. Bacteriol. 171:4448-4456(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF N-TERMINUS.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
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).
RN [6]
RP PHOSPHORYLATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15522865; DOI=10.1074/jbc.m410104200;
RA Yamamoto K., Hirao K., Oshima T., Aiba H., Utsumi R., Ishihama A.;
RT "Functional characterization in vitro of all two-component signal
RT transduction systems from Escherichia coli.";
RL J. Biol. Chem. 280:1448-1456(2005).
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.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by ZraS. {ECO:0000269|PubMed:15522865}.
CC -!- CAUTION: Was originally thought to be involved in the regulation of the
CC labile hydrogenase activity. {ECO:0000305|PubMed:2666400}.
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DR EMBL; M28369; AAA24004.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43102.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76978.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77315.1; -; Genomic_DNA.
DR PIR; G65207; B33862.
DR RefSeq; NP_418432.1; NC_000913.3.
DR RefSeq; WP_000148503.1; NZ_SSZK01000047.1.
DR AlphaFoldDB; P14375; -.
DR SMR; P14375; -.
DR BioGRID; 4262463; 6.
DR DIP; DIP-9980N; -.
DR STRING; 511145.b4004; -.
DR PaxDb; P14375; -.
DR PRIDE; P14375; -.
DR EnsemblBacteria; AAC76978; AAC76978; b4004.
DR EnsemblBacteria; BAE77315; BAE77315; BAE77315.
DR GeneID; 948505; -.
DR KEGG; ecj:JW3968; -.
DR KEGG; eco:b4004; -.
DR PATRIC; fig|1411691.4.peg.2706; -.
DR EchoBASE; EB0477; -.
DR eggNOG; COG2204; Bacteria.
DR HOGENOM; CLU_000445_0_6_6; -.
DR InParanoid; P14375; -.
DR OMA; MPISMQV; -.
DR PhylomeDB; P14375; -.
DR BioCyc; EcoCyc:HYDG-MON; -.
DR PRO; PR:P14375; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IDA:EcoCyc.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:EcoCyc.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
DR GO; GO:0006351; P:transcription, DNA-templated; IEP:EcoCyc.
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 1: Evidence at protein level;
KW Activator; ATP-binding; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..441
FT /note="Transcriptional regulatory protein ZraR"
FT /id="PRO_0000081279"
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"
FT CONFLICT 117..122
FT /note="LEKALA -> WKKRS (in Ref. 1; AAA24004)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="S -> C (in Ref. 1; AAA24004)"
FT /evidence="ECO:0000305"
FT CONFLICT 172..174
FT /note="GTG -> AR (in Ref. 1; AAA24004)"
FT /evidence="ECO:0000305"
FT CONFLICT 181..182
FT /note="AI -> GL (in Ref. 1; AAA24004)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="R -> P (in Ref. 1; AAA24004)"
FT /evidence="ECO:0000305"
FT CONFLICT 237..238
FT /note="LF -> C (in Ref. 1; AAA24004)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..346
FT /note="KAVKGFTPQAM -> RGKRFYAPGL (in Ref. 1; AAA24004)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="A -> G (in Ref. 1; AAA24004)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 48395 MW; A7BAB1372F374DDD CRC64;
MTHDNIDILV VDDDISHCTI LQALLRGWGY NVALANSGRQ ALEQVREQVF DLVLCDVRMA
EMDGIATLKE IKALNPAIPV LIMTAYSSVE TAVEALKTGA LDYLIKPLDF DNLQATLEKA
LAHTHSIDAE TPAVTASQFG MVGKSPAMQH LLSEIALVAP SEATVLIHGD SGTGKELVAR
AIHASSARSE KPLVTLNCAA LNESLLESEL FGHEKGAFTG ADKRREGRFV EADGGTLFLD
EIGDISPMMQ VRLLRAIQER EVQRVGSNQI ISVDVRLIAA THRDLAAEVN AGRFRQDLYY
RLNVVAIEVP SLRQRREDIP LLAGHFLQRF AERNRKAVKG FTPQAMDLLI HYDWPGNIRE
LENAVERAVV LLTGEYISER ELPLAIASTP IPLGQSQDIQ PLVEVEKEVI LAALEKTGGN
KTEAARQLGI TRKTLLAKLS R
