ID   LYSM_SULTO              Reviewed;         140 AA.
AC   Q976J7;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=HTH-type transcriptional regulator LysM;
GN   Name=lysM; OrderedLocusNames=STK_01930;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
CC   -!- FUNCTION: In the absence or at low concentrations of lysine, activates
CC       the biosynthesis of this amino acid via the alpha-aminoadipate (AAA)
CC       pathway. {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway
CC       [regulation].
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR   EMBL; BA000023; BAB65150.1; -; Genomic_DNA.
DR   RefSeq; WP_010978132.1; NC_003106.2.
DR   AlphaFoldDB; Q976J7; -.
DR   SMR; Q976J7; -.
DR   STRING; 273063.STK_01930; -.
DR   EnsemblBacteria; BAB65150; BAB65150; STK_01930.
DR   GeneID; 42799670; -.
DR   KEGG; sto:STK_01930; -.
DR   PATRIC; fig|273063.9.peg.237; -.
DR   eggNOG; arCOG01580; Archaea.
DR   OMA; TYMWGTR; -.
DR   OrthoDB; 97695at2157; -.
DR   UniPathway; UPA00033; -.
DR   Proteomes; UP000001015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR   CDD; cd00090; HTH_ARSR; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011991; ArsR-like_HTH.
DR   InterPro; IPR000485; AsnC-type_HTH_dom.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR019888; Tscrpt_reg_AsnC-like.
DR   InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF01037; AsnC_trans_reg; 1.
DR   PRINTS; PR00033; HTHASNC.
DR   SMART; SM00344; HTH_ASNC; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
DR   PROSITE; PS50956; HTH_ASNC_2; 1.
PE   3: Inferred from homology;
KW   Activator; Cytoplasm; DNA-binding; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..140
FT                   /note="HTH-type transcriptional regulator LysM"
FT                   /id="PRO_0000111743"
FT   DOMAIN          4..67
FT                   /note="HTH asnC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
FT   DNA_BIND        23..42
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
SQ   SEQUENCE   140 AA;  15969 MW;  34D51F029101678B CRC64;
     MADVDESDLK ILEILRKNAR TPYTSIAKEL KISEAAVRKR IEKLIKMGVI KRFTIDYELE
     NEIRAIVMVK TNPQIPTPEI SKKIIKIQGV EFVYETTGDY DILTVVRGTN ISSINKTIDD
     IRSLQGVLST NSTIVLRVWF