16S/23S rRNA (cytidine-2'-O)-methyltransferase TlyA

Details

Name
16S/23S rRNA (cytidine-2'-O)-methyltransferase TlyA
Synonyms
  • 16S rRNA (cytidine1409-2'-O)-methyltransferase
  • 2.1.1.226
  • 23S rRNA (cytidine1920-2'-O)-methyltransferase
  • Hemolysin TlyA
Gene Name
tlyA
UniProtKB Entry
P9WJ63Swiss-Prot
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
NCBI Taxonomy ID
83332
Amino acid sequence
>lcl|BSEQ0052088|16S/23S rRNA (cytidine-2'-O)-methyltransferase TlyA
MARRARVDAELVRRGLARSRQQAAELIGAGKVRIDGLPAVKPATAVSDTTALTVVTDSER
AWVSRGAHKLVGALEAFAIAVAGRRCLDAGASTGGFTEVLLDRGAAHVVAADVGYGQLAW
SLRNDPRVVVLERTNARGLTPEAIGGRVDLVVADLSFISLATVLPALVGCASRDADIVPL
VKPQFEVGKGQVGPGGVVHDPQLRARSVLAVARRAQELGWHSVGVKASPLPGPSGNVEYF
LWLRTQTDRALSAKGLEDAVHRAISEGP
Number of residues
268
Molecular Weight
28073.885
Theoretical pI
Not Available
GO Classification
Functions
RNA binding / rRNA methyltransferase activity / toxin activity
Processes
hemolysis by symbiont of host erythrocytes / rRNA methylation
Components
cell wall / cytoplasm / extracellular region / host cell plasma membrane / membrane
General Function
Acts as a host evasion factor, that significantly contributes to the pathogenesis of M.tuberculosis by modulating adaptive immune responses by inhibiting host-protective Th1 and Th17 cytokine responses as well as autophagy (PubMed:25847237). Catalyzes the 2'-O-methylation at nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA (PubMed:16857584, PubMed:20854656). Is likely involved in ribosomal biogenesis (PubMed:21443791). Also exhibits hemolytic activity in vitro, by binding with and oligomerizing into host cell membranes (PubMed:20854656, PubMed:9611795).
Specific Function
Rna binding
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0052089|16S/23S rRNA (cytidine-2'-O)-methyltransferase TlyA (tlyA)
GTGGCACGACGTGCCCGCGTTGACGCCGAGCTAGTCCGGCGGGGCCTGGCGCGATCACGT
CAACAGGCCGCGGAGTTGATCGGCGCCGGCAAGGTGCGCATCGACGGGCTGCCGGCGGTC
AAGCCGGCCACCGCCGTGTCCGACACCACCGCGCTGACCGTGGTGACCGACAGTGAACGC
GCCTGGGTATCGCGCGGAGCGCACAAACTAGTCGGTGCGCTGGAGGCGTTCGCGATCGCG
GTGGCGGGCCGGCGCTGTCTGGACGCGGGCGCATCGACCGGTGGGTTCACCGAAGTACTG
CTGGACCGTGGTGCCGCCCACGTGGTGGCCGCCGATGTCGGATACGGCCAGCTGGCGTGG
TCGCTGCGCAACGATCCTCGGGTGGTGGTCCTCGAGCGGACCAACGCACGTGGCCTCACA
CCGGAGGCGATCGGCGGTCGCGTCGACCTGGTAGTGGCCGACCTGTCGTTCATCTCGTTG
GCTACCGTGTTGCCCGCGCTGGTTGGATGCGCTTCGCGCGACGCCGATATCGTTCCACTG
GTGAAGCCGCAGTTTGAGGTGGGGAAAGGTCAGGTCGGCCCCGGTGGGGTGGTCCATGAC
CCGCAGTTGCGTGCGCGGTCGGTGCTCGCGGTCGCGCGGCGGGCACAGGAGCTGGGCTGG
CACAGCGTCGGCGTCAAGGCCAGCCCGCTGCCGGGCCCATCGGGCAATGTCGAGTACTTC
CTGTGGTTGCGCACGCAGACCGACCGGGCATTGTCGGCCAAGGGATTGGAGGATGCGGTG
CACCGTGCGATTAGCGAGGGCCCGTAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP9WJ63
UniProtKB Entry NameTLYA_MYCTU
PDB ID(s)5KS2, 5KYG
KEGG IDmtu:Rv1694
NCBI Gene ID885396
General References
  1. Wren BW, Stabler RA, Das SS, Butcher PD, Mangan JA, Clarke JD, Casali N, Parish T, Stoker NG: Characterization of a haemolysin from Mycobacterium tuberculosis with homology to a virulence factor of Serpulina hyodysenteriae. Microbiology. 1998 May;144 ( Pt 5):1205-11. doi: 10.1099/00221287-144-5-1205. [Article]
  2. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
  3. Maus CE, Plikaytis BB, Shinnick TM: Mutation of tlyA confers capreomycin resistance in Mycobacterium tuberculosis. Antimicrob Agents Chemother. 2005 Feb;49(2):571-7. doi: 10.1128/AAC.49.2.571-577.2005. [Article]
  4. Johansen SK, Maus CE, Plikaytis BB, Douthwaite S: Capreomycin binds across the ribosomal subunit interface using tlyA-encoded 2'-O-methylations in 16S and 23S rRNAs. Mol Cell. 2006 Jul 21;23(2):173-82. [Article]
  5. Rahman A, Srivastava SS, Sneh A, Ahmed N, Krishnasastry MV: Molecular characterization of tlyA gene product, Rv1694 of Mycobacterium tuberculosis: a non-conventional hemolysin and a ribosomal RNA methyl transferase. BMC Biochem. 2010 Sep 20;11:35. doi: 10.1186/1471-2091-11-35. [Article]
  6. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
  7. Arenas NE, Salazar LM, Soto CY, Vizcaino C, Patarroyo ME, Patarroyo MA, Gomez A: Molecular modeling and in silico characterization of Mycobacterium tuberculosis TlyA: possible misannotation of this tubercle bacilli-hemolysin. BMC Struct Biol. 2011 Mar 28;11:16. doi: 10.1186/1472-6807-11-16. [Article]
  8. Kumar S, Mittal E, Deore S, Kumar A, Rahman A, Krishnasastry MV: Mycobacterial tlyA gene product is localized to the cell-wall without signal sequence. Front Cell Infect Microbiol. 2015 Aug 21;5:60. doi: 10.3389/fcimb.2015.00060. eCollection 2015. [Article]
  9. Rahman MA, Sobia P, Dwivedi VP, Bhawsar A, Singh DK, Sharma P, Moodley P, Van Kaer L, Bishai WR, Das G: Mycobacterium tuberculosis TlyA Protein Negatively Regulates T Helper (Th) 1 and Th17 Differentiation and Promotes Tuberculosis Pathogenesis. J Biol Chem. 2015 Jun 5;290(23):14407-17. doi: 10.1074/jbc.M115.653600. Epub 2015 Apr 6. [Article]

Associated Data

Bio-Entities
Bio-EntityType
16S/23S rRNA (cytidine-2'-O)-methyltransferase TlyA (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))protein
primary
Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
ViomycinapprovedyestargetinhibitorDetails
CapreomycinapprovedyestargetinhibitorDetails