ID   YJIR_ECOLI              Reviewed;         470 AA.
AC   P39389; Q2M5X4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Uncharacterized HTH-type transcriptional regulator YjiR;
GN   Name=yjiR; OrderedLocusNames=b4340, JW4303;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [2]
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   [3]
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).
CC   -!- SIMILARITY: In the C-terminal section; belongs to the class-I
CC       pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.
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DR   EMBL; U14003; AAA97236.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77296.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78332.1; -; Genomic_DNA.
DR   PIR; S56565; S56565.
DR   RefSeq; NP_418760.1; NC_000913.3.
DR   RefSeq; WP_000199300.1; NZ_LN832404.1.
DR   AlphaFoldDB; P39389; -.
DR   SMR; P39389; -.
DR   BioGRID; 4261620; 18.
DR   IntAct; P39389; 4.
DR   STRING; 511145.b4340; -.
DR   PaxDb; P39389; -.
DR   PRIDE; P39389; -.
DR   EnsemblBacteria; AAC77296; AAC77296; b4340.
DR   EnsemblBacteria; BAE78332; BAE78332; BAE78332.
DR   GeneID; 949089; -.
DR   KEGG; ecj:JW4303; -.
DR   KEGG; eco:b4340; -.
DR   PATRIC; fig|1411691.4.peg.2346; -.
DR   EchoBASE; EB2466; -.
DR   eggNOG; COG1167; Bacteria.
DR   HOGENOM; CLU_017584_0_0_6; -.
DR   InParanoid; P39389; -.
DR   OMA; MPEQIMV; -.
DR   PhylomeDB; P39389; -.
DR   BioCyc; EcoCyc:G7936-MON; -.
DR   PRO; PR:P39389; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR   GO; GO:1901605; P:alpha-amino acid metabolic process; IBA:GO_Central.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd07377; WHTH_GntR; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF00392; GntR; 1.
DR   SMART; SM00345; HTH_GNTR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS50949; HTH_GNTR; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; DNA-binding; Pyridoxal phosphate; Reference proteome;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..470
FT                   /note="Uncharacterized HTH-type transcriptional regulator
FT                   YjiR"
FT                   /id="PRO_0000050709"
FT   DOMAIN          1..69
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT   MOD_RES         313
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   470 AA;  53047 MW;  0C65DA4DC69A4FDA CRC64;
     MTRYQHLATL LAERIEQGLY RHGEKLPSVR SLSQEHGVSI STVQQAYQTL ETMKLITPQP
     RSGYFVAQRK AQPPVPPMTR PVQRPVEITQ WDQVLDMLEA HSDSSIVPLS KSTPDVEAPS
     LKPLWRELSR VVQHNLQTVL GYDLLAGQRV LREQIARLML DSGSVVTADD IIITSGCHNS
     MSLALMAVCK PGDIVAVESP CYYGSMQMLR GMGVKVIEIP TDPETGISVE ALELALEQWP
     IKGIILVPNC NNPLGFIMPD ARKRAVLSLA QRHDIVIFED DVYGELATEY PRPRTIHSWD
     IDGRVLLCSS FSKSIAPGLR VGWVAPGRYH DKLMHMKYAI SSFNVPSTQM AAATFVLEGH
     YHRHIRRMRQ IYQRNLALYT CWIREYFPCE ICITRPKGGF LLWIELPEQV DMVCVARQLC
     RMKIQVAAGS IFSASGKYRN CLRINCALPL SETYREALKQ IGEAVYRAME