ID   LSR2_MYCTO              Reviewed;         112 AA.
AC   P9WIP6; L0TG69; O06285; P65648;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Nucleoid-associated protein Lsr2;
GN   Name=lsr2; OrderedLocusNames=MT3704;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: DNA-bridging protein that has both architectural and
CC       regulatory roles. Influences the organization of chromatin and gene
CC       expression by binding non-specifically to DNA, with a preference for
CC       AT-rich sequences, and bridging distant DNA segments. Represses
CC       expression of multiple genes involved in a broad range of cellular
CC       processes. May coordinate global gene regulation and virulence as well
CC       as genes important for adaptation to changing O(2) levels. Protects
CC       against reactive oxygen intermediates (By similarity).
CC       {ECO:0000250|UniProtKB:P9WIP7}.
CC   -!- SUBUNIT: Homodimer. May form higher oligomers via protease-activation
CC       (By similarity). {ECO:0000250|UniProtKB:P9WIP7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC       {ECO:0000250|UniProtKB:P9WIP7}.
CC   -!- DOMAIN: The C-terminal domain binds DNA and the N-terminal domain is
CC       involved in dimerization. Both domains are essential for normal
CC       function (By similarity). {ECO:0000250|UniProtKB:P9WIP7}.
CC   -!- PTM: The three N-terminal residues may be cleaved by proteases in
CC       response to external stress. This cleavage may be required for
CC       oligomerization, which leads to chromosome compaction and protection
CC       (By similarity). {ECO:0000250|UniProtKB:P9WIP7}.
CC   -!- SIMILARITY: Belongs to the Lsr2 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK48061.1; -; Genomic_DNA.
DR   PIR; F70954; F70954.
DR   RefSeq; WP_003419513.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIP6; -.
DR   BMRB; P9WIP6; -.
DR   SMR; P9WIP6; -.
DR   EnsemblBacteria; AAK48061; AAK48061; MT3704.
DR   GeneID; 45427584; -.
DR   KEGG; mtc:MT3704; -.
DR   PATRIC; fig|83331.31.peg.3986; -.
DR   HOGENOM; CLU_139818_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.60.230; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR024412; Lsr2.
DR   InterPro; IPR042261; Lsr2_dimerization.
DR   Pfam; PF11774; Lsr2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; Repressor; Transcription; Transcription regulation;
KW   Virulence.
FT   CHAIN           1..112
FT                   /note="Nucleoid-associated protein Lsr2"
FT                   /id="PRO_0000427968"
FT   DNA_BIND        97..102
FT                   /evidence="ECO:0000250|UniProtKB:P9WIP7"
FT   REGION          57..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   112 AA;  12098 MW;  A4B32E478CBAC3E4 CRC64;
     MAKKVTVTLV DDFDGSGAAD ETVEFGLDGV TYEIDLSTKN ATKLRGDLKQ WVAAGRRVGG
     RRRGRSGSGR GRGAIDREQS AAIREWARRN GHNVSTRGRI PADVIDAYHA AT