LSR2_MYCBO
ID LSR2_MYCBO Reviewed; 112 AA.
AC P65649; A0A1R3Y683; O06285; X2BP54;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Nucleoid-associated protein Lsr2;
GN Name=lsr2; OrderedLocusNames=BQ2027_MB3628C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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. {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; LT708304; SIU02255.1; -; Genomic_DNA.
DR RefSeq; NP_857267.1; NC_002945.3.
DR RefSeq; WP_003419513.1; NC_002945.4.
DR AlphaFoldDB; P65649; -.
DR BMRB; P65649; -.
DR SMR; P65649; -.
DR EnsemblBacteria; SIU02255; SIU02255; BQ2027_MB3628C.
DR GeneID; 45427584; -.
DR PATRIC; fig|233413.5.peg.3974; -.
DR OMA; PIREWAR; -.
DR Proteomes; UP000001419; 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_0000021623"
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