Small　protein　B　(SmpB)　is　an　essential　molecule　in　trans-translation　which　is　a　universal　biological　pathway　for　protein　synthesis　in　bacteria.　Trans-translation　can　release　stalled　ribosomes　from　defective　mRNAs　and　target　tag-protein　fragments　for　degradation,　and　then　restart　protein　synthesis.　The　SmpB-tmRNA　complex　coordinating　with　other　components　of　the　trans-translation　system,　plays　vital　roles　in　Mycobacterium　tuberculosis　under　both　stress　conditions　and　non-replicating　conditions.　Thus,　elucidation　of　molecular　details　and　dynamic　properties　of　the　SmpB-tmRNA　interaction　is　a　crucial　step　towards　effectively　blocking　trans-translation　process　to　shorten　the　duration　of　tuberculosis　treatment.　Here,　we　report　resonance　assignments　for　H-1,　C-13　and　N-15　of　M.　tuberculosis　SmpB　(MtSmpB,　spanning　residues　4-133)　protein　determined　by　a　suite　of　2D/3D　heteronuclear　NMR　experiments　along　with　predicted　the　secondary　structure.