ID   LSR2_MYCLE              Reviewed;         112 AA.
AC   P24094;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Nucleoid-associated protein Lsr2 {ECO:0000303|PubMed:1992456};
DE   AltName: Full=15 kDa antigen;
DE   AltName: Full=A15 {ECO:0000303|PubMed:1840579};
GN   Name=lsr2; OrderedLocusNames=ML0234;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=1840579; DOI=10.1128/iai.59.11.4117-4124.1991;
RA   Sela S., Thole J.E., Ottenhoff T.H., Clark-Curtiss J.E.;
RT   "Identification of Mycobacterium leprae antigens from a cosmid library:
RT   characterization of a 15-kilodalton antigen that is recognized by both the
RT   humoral and cellular immune systems in leprosy patients.";
RL   Infect. Immun. 59:4117-4124(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-112, AND FUNCTION.
RX   PubMed=1992456; DOI=10.1073/pnas.88.3.1054;
RA   Laal S., Sharma Y.D., Prasad H.K., Murtaza A., Singh S., Tangri S.,
RA   Misra R.S., Nath I.;
RT   "Recombinant fusion protein identified by lepromatous sera mimics native
RT   Mycobacterium leprae in T-cell responses across the leprosy spectrum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:1054-1058(1991).
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). Dominant T-cell
CC       antigen and stimulates lymphoproliferation. Most probably causes the
CC       lymphoproliferative responses occurring in leprosy.
CC       {ECO:0000250|UniProtKB:P9WIP7, ECO:0000269|PubMed:1840579,
CC       ECO:0000269|PubMed:1992456}.
CC   -!- SUBUNIT: Homodimer. {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   -!- SIMILARITY: Belongs to the Lsr2 family. {ECO:0000305}.
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DR   EMBL; M67510; AAA25351.1; -; Genomic_DNA.
DR   EMBL; AL583917; CAC29742.1; -; Genomic_DNA.
DR   EMBL; X53487; CAA37572.1; -; Genomic_DNA.
DR   PIR; B43601; B43601.
DR   RefSeq; NP_301294.1; NC_002677.1.
DR   RefSeq; WP_010907618.1; NC_002677.1.
DR   AlphaFoldDB; P24094; -.
DR   BMRB; P24094; -.
DR   SMR; P24094; -.
DR   STRING; 272631.ML0234; -.
DR   EnsemblBacteria; CAC29742; CAC29742; CAC29742.
DR   KEGG; mle:ML0234; -.
DR   PATRIC; fig|272631.5.peg.367; -.
DR   Leproma; ML0234; -.
DR   eggNOG; ENOG5032RKK; Bacteria.
DR   HOGENOM; CLU_139818_0_0_11; -.
DR   OMA; PIREWAR; -.
DR   Proteomes; UP000000806; 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; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Virulence.
FT   CHAIN           1..112
FT                   /note="Nucleoid-associated protein Lsr2"
FT                   /id="PRO_0000021624"
FT   DNA_BIND        97..102
FT                   /evidence="ECO:0000250|UniProtKB:P9WIP7"
FT   REGION          58..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   112 AA;  12165 MW;  B4CD4D7C0D9F00A1 CRC64;
     MAKKVTVTLV DDFDGAGAAD ETVEFGLDGV TYEIDLTNKN AAKLRGDLRQ WVSAGRRVGG
     RRRGRSNSGR GRGAIDREQS AAIREWARRN GHNVSTRGRI PADVIDAFHA AT