| IED ID |
IndEnz0002006081 |
| Enzyme Type ID |
protease006081 |
| Protein Name |
Nucleoid-associated protein Lsr2
|
| Gene Name |
lsr2 Rv3597c MTCY07H7B.25 |
| Organism |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Taxonomic Lineage |
cellular organisms
Bacteria
Terrabacteria group
Actinobacteria
Actinomycetia (high G+C Gram-positive bacteria)
Corynebacteriales
Mycobacteriaceae
Mycobacterium
Mycobacterium tuberculosis complex
Mycobacterium tuberculosis
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
|
| Enzyme Sequence |
MAKKVTVTLVDDFDGSGAADETVEFGLDGVTYEIDLSTKNATKLRGDLKQWVAAGRRVGGRRRGRSGSGRGRGAIDREQSAAIREWARRNGHNVSTRGRIPADVIDAYHAAT |
| Enzyme Length |
112 |
| Uniprot Accession Number |
P9WIP7 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
DNA_BIND 97..102; /evidence=ECO:0000305|PubMed:21673140 |
| EC Number |
|
| Enzyme Function |
FUNCTION: DNA-bridging protein that has both architectural and regulatory roles (PubMed:18187505). Influences the organization of chromatin and gene expression by binding non-specifically to DNA, with a preference for AT-rich sequences, and bridging distant DNA segments (PubMed:20133735). Binds in the minor groove of AT-rich DNA (PubMed:21673140). Represses expression of multiple genes involved in a broad range of cellular processes, including major virulence factors or antibiotic-induced genes, such as iniBAC or efpA (PubMed:17590082), and genes important for adaptation of changing O(2) levels (PubMed:24895305). May also activate expression of some gene (PubMed:24895305). May coordinate global gene regulation and virulence (PubMed:20133735). Also protects mycobacteria against reactive oxygen intermediates during macrophage infection by acting as a physical barrier to DNA degradation (PubMed:19237572); the physical protection has been questioned (PubMed:24895305). A strain overexpressing this protein consumes O(2) more slowly than wild-type (PubMed:24895305). {ECO:0000269|PubMed:17590082, ECO:0000269|PubMed:18187505, ECO:0000269|PubMed:19237572, ECO:0000269|PubMed:20133735, ECO:0000269|PubMed:21673140, ECO:0000269|PubMed:24895305}. |
| Temperature Dependency |
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| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Beta strand (6); Chain (1); DNA binding (1); Helix (4); Mutagenesis (7); Region (1); Turn (1) |
| Keywords |
3D-structure;Cytoplasm;DNA-binding;Reference proteome;Repressor;Transcription;Transcription regulation;Virulence |
| Interact With |
|
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:18187505, ECO:0000269|PubMed:20133735}. |
| Modified Residue |
|
| Post Translational Modification |
PTM: The three N-terminal residues may be cleaved by proteases in response to external stress. This cleavage may be required for oligomerization, which leads to chromosome compaction and protection. {ECO:0000269|PubMed:22719899}. |
| Signal Peptide |
|
| Structure 3D |
NMR spectroscopy (3); X-ray crystallography (2) |
| Cross Reference PDB |
2KNG;
4E1P;
4E1R;
6QKP;
6QKQ;
|
| Mapped Pubmed ID |
31562654;
|
| Motif |
|
| Gene Encoded By |
|
| Mass |
12,098 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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