ID   NHAR_ECOLI              Reviewed;         301 AA.
AC   P0A9G2; P10087; P75619; Q2MCH4; Q47409; Q83SR2;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Transcriptional activator protein NhaR;
DE   AltName: Full=Na(+)/H(+) antiporter regulatory protein;
GN   Name=nhaR; Synonyms=antO; OrderedLocusNames=b0020, JW0019;
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=2429258; DOI=10.1093/nar/14.17.6965;
RA   Mackie G.A.;
RT   "Structure of the DNA distal to the gene for ribosomal protein S20 in
RT   Escherichia coli K12: presence of a strong terminator and an IS1 element.";
RL   Nucleic Acids Res. 14:6965-6981(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Harel O.;
RT   "NhaR, a regulator of nhaA.";
RL   Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA   Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA   Mizobuchi K., Nakata A.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT   2.4 min region.";
RL   Nucleic Acids Res. 20:3305-3308(1992).
RN   [4]
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   [5]
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   [6]
RP   IDENTIFICATION OF PROTEIN, AND POSSIBLE DNA-BINDING REGION.
RX   PubMed=3413113; DOI=10.1073/pnas.85.18.6602;
RA   Henikoff S., Haughn G.W., Calvo J.M., Wallace J.C.;
RT   "A large family of bacterial activator proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:6602-6606(1988).
RN   [7]
RP   FUNCTION.
RX   PubMed=1316901; DOI=10.1016/s0021-9258(19)50037-0;
RA   Rahav-Manor O., Carmel O., Karpel R., Taglicht D., Glaser G.,
RA   Schuldiner S., Padan E.;
RT   "NhaR, a protein homologous to a family of bacterial regulatory proteins
RT   (LysR), regulates nhaA, the sodium proton antiporter gene in Escherichia
RT   coli.";
RL   J. Biol. Chem. 267:10433-10438(1992).
RN   [8]
RP   VARIANT NHAR1.
RX   PubMed=8168494; DOI=10.1002/j.1460-2075.1994.tb06467.x;
RA   Carmel O., Dover N., Rahav-Manor O., Dibrov P., Kirsch D., Karpel R.,
RA   Schuldiner S., Padan E.;
RT   "A single amino acid substitution (Glu134-->Ala) in NhaR1 increases the
RT   inducibility by Na+ of the product of nhaA, a Na+/H+ antiporter gene in
RT   Escherichia coli.";
RL   EMBO J. 13:1981-1989(1994).
CC   -!- FUNCTION: Plays a role in the positive regulation of NhaA.
CC       {ECO:0000269|PubMed:1316901}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
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DR   EMBL; X04382; CAA27969.1; -; Genomic_DNA.
DR   EMBL; L24072; AAA24221.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73131.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76032.1; -; Genomic_DNA.
DR   RefSeq; NP_414561.1; NC_000913.3.
DR   RefSeq; WP_000062890.1; NZ_CP047127.1.
DR   AlphaFoldDB; P0A9G2; -.
DR   SMR; P0A9G2; -.
DR   BioGRID; 4259724; 3.
DR   IntAct; P0A9G2; 2.
DR   STRING; 511145.b0020; -.
DR   jPOST; P0A9G2; -.
DR   PaxDb; P0A9G2; -.
DR   PRIDE; P0A9G2; -.
DR   EnsemblBacteria; AAC73131; AAC73131; b0020.
DR   EnsemblBacteria; BAE76032; BAE76032; BAE76032.
DR   GeneID; 944757; -.
DR   KEGG; ecj:JW0019; -.
DR   KEGG; eco:b0020; -.
DR   PATRIC; fig|511145.12.peg.17; -.
DR   EchoBASE; EB1070; -.
DR   eggNOG; COG0583; Bacteria.
DR   HOGENOM; CLU_039613_9_0_6; -.
DR   InParanoid; P0A9G2; -.
DR   OMA; WLNYHHL; -.
DR   PhylomeDB; P0A9G2; -.
DR   BioCyc; EcoCyc:PD00474; -.
DR   PHI-base; PHI:3267; -.
DR   PRO; PR:P0A9G2; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:EcoCyc.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IMP:EcoCyc.
DR   GO; GO:2000142; P:regulation of DNA-templated transcription, initiation; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR005119; LysR_subst-bd.
DR   InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00126; HTH_1; 1.
DR   Pfam; PF03466; LysR_substrate; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50931; HTH_LYSR; 1.
PE   1: Evidence at protein level;
KW   Activator; Cytoplasm; DNA-binding; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..301
FT                   /note="Transcriptional activator protein NhaR"
FT                   /id="PRO_0000105689"
FT   DOMAIN          6..63
FT                   /note="HTH lysR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   DNA_BIND        23..42
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   MUTAGEN         134
FT                   /note="E->A: In nhaR1; increases the transcription of
FT                   NhaA."
FT   CONFLICT        46..47
FT                   /note="ER -> DA (in Ref. 1, 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50
FT                   /note="G -> A (in Ref. 1, 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        58..65
FT                   /note="RGLEPSEL -> TWSRTQRA (in Ref. 1 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        146
FT                   /note="D -> E (in Ref. 1, 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        233..301
FT                   /note="FGAMHNAIFVAPTLYAYDFYADKTVVEIGRVENVMEEYHAIFAERMIQHPAV
FT                   QRICNTDYSALFSPAVR -> WLQVLLVAMQMQSSLPQRFMHMTFMPIKLS (in
FT                   Ref. 1 and 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   301 AA;  34284 MW;  E81FAFC4FC4FD2F1 CRC64;
     MSMSHINYNH LYYFWHVYKE GSVVGAAEAL YLTPQTITGQ IRALEERLQG KLFKRKGRGL
     EPSELGELVY RYADKMFTLS QEMLDIVNYR KESNLLFDVG VADALSKRLV SSVLNAAVVE
     GEPIHLRCFE STHEMLLEQL SQHKLDMIIS DCPIDSTQQE GLFSVRIGEC GVSFWCTNPP
     PEKPFPACLE ERRLLIPGRR SMLGRKLLNW FNSQGLNVEI LGEFDDAALM KAFGAMHNAI
     FVAPTLYAYD FYADKTVVEI GRVENVMEEY HAIFAERMIQ HPAVQRICNT DYSALFSPAV
     R