ID   LYSM_SACS2              Reviewed;         142 AA.
AC   Q980W9;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=HTH-type transcriptional regulator LysM;
GN   Name=lysM; OrderedLocusNames=SSO0157;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2]
RP   FUNCTION IN LYSINE BIOSYNTHESIS, INDUCTION, AND SUBUNIT.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=12042311; DOI=10.1074/jbc.m203528200;
RA   Brinkman A.B., Bell S.D., Lebbink R.J., de Vos W.M., van der Oost J.;
RT   "The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine
RT   biosynthesis in response to lysine availability.";
RL   J. Biol. Chem. 277:29537-29549(2002).
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:0000269|PubMed:12042311}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway
CC       [regulation].
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12042311}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:12042311}.
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DR   EMBL; AE006641; AAK40503.1; -; Genomic_DNA.
DR   EMBL; BK000545; DAA00051.1; -; Genomic_DNA.
DR   PIR; H90155; H90155.
DR   RefSeq; WP_009990382.1; NC_002754.1.
DR   AlphaFoldDB; Q980W9; -.
DR   SMR; Q980W9; -.
DR   STRING; 273057.SSO0157; -.
DR   EnsemblBacteria; AAK40503; AAK40503; SSO0157.
DR   GeneID; 44129119; -.
DR   KEGG; sso:SSO0157; -.
DR   PATRIC; fig|273057.12.peg.154; -.
DR   eggNOG; arCOG01580; Archaea.
DR   HOGENOM; CLU_091233_5_3_2; -.
DR   InParanoid; Q980W9; -.
DR   OMA; TYMWGTR; -.
DR   PhylomeDB; Q980W9; -.
DR   UniPathway; UPA00033; -.
DR   Proteomes; UP000001974; 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   1: Evidence at protein level;
KW   Activator; Cytoplasm; DNA-binding; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..142
FT                   /note="HTH-type transcriptional regulator LysM"
FT                   /id="PRO_0000111742"
FT   DOMAIN          6..69
FT                   /note="HTH asnC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
FT   DNA_BIND        25..44
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
SQ   SEQUENCE   142 AA;  16096 MW;  6AEBF0220E6A727A CRC64;
     MGNANIDESD LKILEILKKN ARTPYTLIAK ELKVSEAAIR KRIEKLIRQG IIKRFTIEYE
     LENEIRAIVM VQSTPQIPTP EISKKIAKIP GVEVVYETTG DYDILVIVRG TNITSINRTI
     DEIRSIQGVV GTNSTIILRT WF