FIXJ_RHIME
ID FIXJ_RHIME Reviewed; 204 AA.
AC P10958;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Transcriptional regulatory protein FixJ;
GN Name=fixJ; OrderedLocusNames=RA0669; ORFNames=SMa1227;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymA (megaplasmid 1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2842062; DOI=10.1016/s0092-8674(88)80012-6;
RA David M., Daveran M.-L., Batut J., Dedieu A., Domergue O., Ghai J.,
RA Hertig C., Boistard P., Kahn D.;
RT "Cascade regulation of nif gene expression in Rhizobium meliloti.";
RL Cell 54:671-683(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481432; DOI=10.1073/pnas.161294798;
RA Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA Long S.R.;
RT "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT meliloti pSymA megaplasmid.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 200-204.
RX PubMed=2663474; DOI=10.1002/j.1460-2075.1989.tb03502.x;
RA Batut J., Daveran-Mingot M.-L., David M., Jacobs J., Garnerone A.-M.,
RA Kahn D.;
RT "fixK, a gene homologous with fnr and crp from Escherichia coli, regulates
RT nitrogen fixation genes both positively and negatively in Rhizobium
RT meliloti.";
RL EMBO J. 8:1279-1286(1989).
RN [5]
RP REVIEW, AND MUTAGENESIS OF HTH REGION.
RX PubMed=1857213; DOI=10.1111/j.1365-2958.1991.tb00774.x;
RA Kahn D., Ditta G.S.;
RT "Modular structure of FixJ: homology of the transcriptional activator
RT domain with the -35 binding domain of sigma factors.";
RL Mol. Microbiol. 5:987-997(1991).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-126.
RX PubMed=10647182; DOI=10.1016/s0969-2126(00)88342-2;
RA Gouet P., Fabry B., Guillet V., Birck C., Mourey L., Kahn D., Samama J.-P.;
RT "Structural transitions in the FixJ receiver domain.";
RL Structure 7:1517-1526(1999).
CC -!- FUNCTION: FixJ, when activated by FixL, induces the expression of both
CC nifA, required for activation of classical nif and fix genes, and fixK,
CC required for FixN activation.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by FixL.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z21854; CAA79898.1; -; Genomic_DNA.
DR EMBL; AE006469; AAK65327.1; -; Genomic_DNA.
DR EMBL; X15079; CAA33182.1; -; Genomic_DNA.
DR PIR; B31227; B31227.
DR PIR; E95345; E95345.
DR RefSeq; NP_435915.1; NC_003037.1.
DR RefSeq; WP_010967648.1; NC_003037.1.
DR PDB; 1D5W; X-ray; 2.30 A; A/B/C=1-124.
DR PDB; 1DBW; X-ray; 1.60 A; A/B=1-124.
DR PDB; 1DCK; X-ray; 2.00 A; A/B=1-124.
DR PDB; 1DCM; X-ray; 3.00 A; A/B=1-124.
DR PDB; 1X3U; NMR; -; A=130-204.
DR PDBsum; 1D5W; -.
DR PDBsum; 1DBW; -.
DR PDBsum; 1DCK; -.
DR PDBsum; 1DCM; -.
DR PDBsum; 1X3U; -.
DR AlphaFoldDB; P10958; -.
DR SMR; P10958; -.
DR EnsemblBacteria; AAK65327; AAK65327; SMa1227.
DR GeneID; 25011576; -.
DR GeneID; 61599437; -.
DR KEGG; sme:SMa1227; -.
DR PATRIC; fig|266834.11.peg.689; -.
DR HOGENOM; CLU_000445_90_4_5; -.
DR OMA; MCRRAFK; -.
DR EvolutionaryTrace; P10958; -.
DR PRO; PR:P10958; -.
DR Proteomes; UP000001976; Plasmid pSymA.
DR CollecTF; EXPREG_00000900; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IPI:CollecTF.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEP:CollecTF.
DR CDD; cd06170; LuxR_C_like; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00196; GerE; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00038; HTHLUXR.
DR SMART; SM00421; HTH_LUXR; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS00622; HTH_LUXR_1; 1.
DR PROSITE; PS50043; HTH_LUXR_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Magnesium; Metal-binding;
KW Nitrogen fixation; Phosphoprotein; Plasmid; Reference proteome;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..204
FT /note="Transcriptional regulatory protein FixJ"
FT /id="PRO_0000081102"
FT DOMAIN 5..119
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 135..200
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT DNA_BIND 159..178
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:1DBW"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:1DBW"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1DBW"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:1DBW"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1DBW"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1DBW"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1DCK"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:1DBW"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1DBW"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:1DBW"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:1DBW"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:1DBW"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:1X3U"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:1X3U"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:1X3U"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:1X3U"
FT HELIX 170..183
FT /evidence="ECO:0007829|PDB:1X3U"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:1X3U"
SQ SEQUENCE 204 AA; 22219 MW; 2EDA356967352292 CRC64;
MTDYTVHIVD DEEPVRKSLA FMLTMNGFAV KMHQSAEAFL AFAPDVRNGV LVTDLRMPDM
SGVELLRNLG DLKINIPSIV ITGHGDVPMA VEAMKAGAVD FIEKPFEDTV IIEAIERASE
HLVAAEADVD DANDIRARLQ TLSERERQVL SAVVAGLPNK SIAYDLDISP RTVEVHRANV
MAKMKAKSLP HLVRMALAGG FGPS
