YDEL_BACSU
ID YDEL_BACSU Reviewed; 463 AA.
AC P96669; Q797H9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Uncharacterized HTH-type transcriptional regulator YdeL;
GN Name=ydeL; OrderedLocusNames=BSU05240;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT subtilis genome.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP GENE FAMILY.
RX PubMed=12123465; DOI=10.1046/j.1365-2958.2002.03036.x;
RA Belitsky B.R., Sonenshein A.L.;
RT "GabR, a member of a novel protein family, regulates the utilization of
RT gamma-aminobutyrate in Bacillus subtilis.";
RL Mol. Microbiol. 45:569-583(2002).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
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; AB001488; BAA19359.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12331.1; -; Genomic_DNA.
DR PIR; F69778; F69778.
DR RefSeq; NP_388405.1; NC_000964.3.
DR RefSeq; WP_003234223.1; NZ_JNCM01000031.1.
DR AlphaFoldDB; P96669; -.
DR SMR; P96669; -.
DR IntAct; P96669; 17.
DR STRING; 224308.BSU05240; -.
DR PaxDb; P96669; -.
DR PRIDE; P96669; -.
DR EnsemblBacteria; CAB12331; CAB12331; BSU_05240.
DR GeneID; 939904; -.
DR KEGG; bsu:BSU05240; -.
DR PATRIC; fig|224308.179.peg.559; -.
DR eggNOG; COG1167; Bacteria.
DR InParanoid; P96669; -.
DR OMA; AFPITNW; -.
DR PhylomeDB; P96669; -.
DR BioCyc; BSUB:BSU05240-MON; -.
DR Proteomes; UP000001570; 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; IEA:UniProtKB-KW.
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 InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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 PRINTS; PR00035; HTHGNTR.
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..463
FT /note="Uncharacterized HTH-type transcriptional regulator
FT YdeL"
FT /id="PRO_0000360696"
FT DOMAIN 13..81
FT /note="HTH gntR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT DNA_BIND 41..60
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT MOD_RES 308
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 463 AA; 53525 MW; DBB7BA2C5D2EF8B7 CRC64;
MDITPFLNRT LDIPLYQQLY RYFKENMHRG RIQKGMKLPS KRLLANQLSI SQTTVERAYE
QLAAEGYIVS KPRSGWFADY HDSDFAYDRM PSTTPIQQEA EENKQWIDFH YGNVDSSYFP
FSAWRKSMVN SLDQYGHELY RPGHVLGEFE LRTLIAEYLY QSRGVHCGPE QVIIGAGNPI
LLQILCQVFE PNISIGYEDP GYPRARKIFE ANRMNIVPIP VDDEGICIQK IKEQQPNLVY
VTPSHQFTLG TIMTINRRIQ LLKWAAENQS FIIEDDYDGE FRYTGQPVPS LQGLDQHNRV
IYMGTFSKSL LPSLRISYMI LPSPLLKKGH EITSLYKQTV SCHSQLTLAE FIKNGEWQKH
INRMRKLYRK KRAIVLEAVQ RELGEHVRIR GENSGLRILL DVYLPFGEKE LIEKAKKHGV
KIYPVSLSYQ HHPPTKTVSL GFAGVSESDI REGIKKLKAA WKI