ID   YDCR_ECOLI              Reviewed;         468 AA.
AC   P77730;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Uncharacterized HTH-type transcriptional regulator YdcR;
GN   Name=ydcR; OrderedLocusNames=b1439, JW1434;
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 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
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; U00096; AAC74521.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15069.1; -; Genomic_DNA.
DR   PIR; B64896; B64896.
DR   RefSeq; NP_415956.1; NC_000913.3.
DR   RefSeq; WP_000760626.1; NZ_SSZK01000021.1.
DR   AlphaFoldDB; P77730; -.
DR   SMR; P77730; -.
DR   BioGRID; 4260188; 15.
DR   DIP; DIP-28077N; -.
DR   IntAct; P77730; 3.
DR   STRING; 511145.b1439; -.
DR   jPOST; P77730; -.
DR   PaxDb; P77730; -.
DR   PRIDE; P77730; -.
DR   EnsemblBacteria; AAC74521; AAC74521; b1439.
DR   EnsemblBacteria; BAA15069; BAA15069; BAA15069.
DR   GeneID; 946004; -.
DR   KEGG; ecj:JW1434; -.
DR   KEGG; eco:b1439; -.
DR   PATRIC; fig|1411691.4.peg.829; -.
DR   EchoBASE; EB3524; -.
DR   eggNOG; COG1167; Bacteria.
DR   HOGENOM; CLU_017584_0_0_6; -.
DR   InParanoid; P77730; -.
DR   OMA; MRLNFTY; -.
DR   PhylomeDB; P77730; -.
DR   BioCyc; EcoCyc:G6750-MON; -.
DR   PRO; PR:P77730; -.
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..468
FT                   /note="Uncharacterized HTH-type transcriptional regulator
FT                   YdcR"
FT                   /id="PRO_0000050708"
FT   DOMAIN          1..69
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT   MOD_RES         312
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   468 AA;  52793 MW;  435A09262FCF79C9 CRC64;
     MKKYQQLAEQ LREQIASGIW QPGDRLPSLR DQVALSGMSF MTVSHAYQLL ESQGYIIARP
     QSGYYVAPQA IKMPKAPVIP VTRDEAVDIN TYIFDMLQAS RDPSVVPFAS AFPDPRLFPL
     QQLNRSLAQV SKTATAMSVI ENLPPGNAEL RQAIARRYAL QGITISPDEI VITAGALEAL
     NLSLQAVTEP GDWVIVENPC FYGALQALER LRLKALSVAT DVKEGIDLQA LELALQEYPV
     KACWLMTNSQ NPLGFTLTPQ KKAQLVALLN QYNVTLIEDD VYSELYFGRE KPLPAKAWDR
     HDGVLHCSSF SKCLVPGFRI GWVAAGKHAR KIQRLQLMST LSTSSPMQLA LVDYLSTRRY
     DAHLRRLRRQ LAERKQRAWQ ALLRYLPAEV KIHHNDSGYF LWLELPEPLD AGELSLAALT
     HHISIAPGKM FSTGENWSRF FRFNTAWQWG EREEQAVKQL GKLIQERL