UniProtKB - P9WJ63 (TLYA_MYCTU)
Protein
16S/23S rRNA (cytidine-2'-O)-methyltransferase TlyA
Gene
tlyA
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
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).5 Publications
Catalytic activityi
- cytidine1409 in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine1409 in 16S rRNA + H+ + S-adenosyl-L-homocysteine1 PublicationEC:2.1.1.2271 Publication
- cytidine1920 in 23S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine1920 in 23S rRNA + H+ + S-adenosyl-L-homocysteine1 PublicationEC:2.1.1.2261 Publication
GO - Molecular functioni
- RNA binding Source: UniProtKB-KW
- rRNA methyltransferase activity Source: MTBBASE
- toxin activity Source: UniProtKB-KW
GO - Biological processi
- hemolysis by symbiont of host erythrocytes Source: MTBBASE
- pathogenesis Source: UniProtKB-KW
- rRNA methylation Source: MTBBASE
Keywordsi
Molecular function | Methyltransferase, RNA-binding, Toxin, Transferase |
Biological process | Cytolysis, Hemolysis, Ribosome biogenesis, rRNA processing, Virulence |
Ligand | S-adenosyl-L-methionine |
Enzyme and pathway databases
BioCyci | MetaCyc:G185E-5885-MONOMER |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:tlyA Ordered Locus Names:Rv1694 |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv1694 |
Subcellular locationi
- Cytoplasm 1 Publication
- cell wall 1 Publication
- Host cell membrane 1 Publication Note: Can bind to target membranes such as macrophage phagosomal membranes (PubMed:20854656). In native and recombinant hosts (M.smegmatis and E.coli), M.tuberculosis TlyA can reach the bacterial surface in functional form and colocalizes with the HBHA protein which is known to be part of cell-wall (PubMed:26347855). TlyA does not seem to depend on either Tat or Sec pathways for translocation to cell-wall (PubMed:26347855). Appears to be capable of reaching the extra-cellular milieu using a vesicle mediated transport (PubMed:26347855).2 Publications
GO - Cellular componenti
- cell wall Source: UniProtKB-SubCell
- cytoplasm Source: UniProtKB-SubCell
- extracellular region Source: UniProtKB-KW
- host cell plasma membrane Source: UniProtKB-SubCell
- membrane Source: UniProtKB-KW
Keywords - Cellular componenti
Cell wall, Cytoplasm, Host cell membrane, Host membrane, Membrane, SecretedPathology & Biotechi
Disruption phenotypei
Cells lacking this gene induce increased IL-12 and reduced IL-1beta and IL-10 cytokine responses, which sharply contrasts with the immune responses induced by wild-type M.tuberculosis (PubMed:25847237). They are also more susceptible to autophagy in macrophages (PubMed:25847237). Consequently, animals infected with the TlyA-deficient mutant M.tuberculosis organisms exhibit increased host-protective immune responses, reduced bacillary load, and increased survival compared with animals infected with wild-type M.tuberculosis (PubMed:25847237). Disruption of this gene leads to capreomycin resistance (PubMed:15673735).2 Publications
Chemistry databases
DrugBanki | DB00314, Capreomycin DB06827, Viomycin |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000415501 | 1 – 268 | 16S/23S rRNA (cytidine-2'-O)-methyltransferase TlyAAdd BLAST | 268 |
Proteomic databases
PaxDbi | P9WJ63 |
Interactioni
Subunit structurei
Can form oligomers on macrophage phagosomal membranes.
1 PublicationProtein-protein interaction databases
STRINGi | 83332.Rv1694 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P9WJ63 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 5 – 67 | S4 RNA-bindingPROSITE-ProRule annotationAdd BLAST | 63 |
Sequence similaritiesi
Belongs to the TlyA family.Curated
Phylogenomic databases
eggNOGi | COG1189, Bacteria |
OMAi | VLMVKPQ |
PhylomeDBi | P9WJ63 |
Family and domain databases
CDDi | cd00165, S4, 1 hit |
Gene3Di | 3.10.290.10, 1 hit |
InterProi | View protein in InterPro IPR004538, Haemolysin_A/TlyA IPR002877, rRNA_MeTrfase_FtsJ_dom IPR002942, S4_RNA-bd IPR036986, S4_RNA-bd_sf IPR029063, SAM-dependent_MTases |
PANTHERi | PTHR32319:SF0, PTHR32319:SF0, 1 hit |
Pfami | View protein in Pfam PF01728, FtsJ, 1 hit PF01479, S4, 1 hit |
PIRSFi | PIRSF005578, TlyA, 1 hit |
SMARTi | View protein in SMART SM00363, S4, 1 hit |
SUPFAMi | SSF53335, SSF53335, 1 hit |
TIGRFAMsi | TIGR00478, tly, 1 hit |
PROSITEi | View protein in PROSITE PS50889, S4, 1 hit |
i Sequence
Sequence statusi: Complete.
P9WJ63-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MARRARVDAE LVRRGLARSR QQAAELIGAG KVRIDGLPAV KPATAVSDTT
60 70 80 90 100
ALTVVTDSER AWVSRGAHKL VGALEAFAIA VAGRRCLDAG ASTGGFTEVL
110 120 130 140 150
LDRGAAHVVA ADVGYGQLAW SLRNDPRVVV LERTNARGLT PEAIGGRVDL
160 170 180 190 200
VVADLSFISL ATVLPALVGC ASRDADIVPL VKPQFEVGKG QVGPGGVVHD
210 220 230 240 250
PQLRARSVLA VARRAQELGW HSVGVKASPL PGPSGNVEYF LWLRTQTDRA
260
LSAKGLEDAV HRAISEGP
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X98295 Genomic DNA Translation: CAA66941.1 AL123456 Genomic DNA Translation: CCP44459.1 |
PIRi | E70502 |
RefSeqi | NP_216210.1, NC_000962.3 WP_003408382.1, NZ_NVQJ01000010.1 |
Genome annotation databases
EnsemblBacteriai | CCP44459; CCP44459; Rv1694 |
GeneIDi | 23492139 885396 |
KEGGi | mtu:Rv1694 mtv:RVBD_1694 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X98295 Genomic DNA Translation: CAA66941.1 AL123456 Genomic DNA Translation: CCP44459.1 |
PIRi | E70502 |
RefSeqi | NP_216210.1, NC_000962.3 WP_003408382.1, NZ_NVQJ01000010.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5KS2 | X-ray | 2.18 | A | 60-268 | [»] | |
5KYG | X-ray | 1.90 | A | 60-268 | [»] | |
SMRi | P9WJ63 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv1694 |
Chemistry databases
DrugBanki | DB00314, Capreomycin DB06827, Viomycin |
Proteomic databases
PaxDbi | P9WJ63 |
Genome annotation databases
EnsemblBacteriai | CCP44459; CCP44459; Rv1694 |
GeneIDi | 23492139 885396 |
KEGGi | mtu:Rv1694 mtv:RVBD_1694 |
Organism-specific databases
TubercuListi | Rv1694 |
Phylogenomic databases
eggNOGi | COG1189, Bacteria |
OMAi | VLMVKPQ |
PhylomeDBi | P9WJ63 |
Enzyme and pathway databases
BioCyci | MetaCyc:G185E-5885-MONOMER |
Family and domain databases
CDDi | cd00165, S4, 1 hit |
Gene3Di | 3.10.290.10, 1 hit |
InterProi | View protein in InterPro IPR004538, Haemolysin_A/TlyA IPR002877, rRNA_MeTrfase_FtsJ_dom IPR002942, S4_RNA-bd IPR036986, S4_RNA-bd_sf IPR029063, SAM-dependent_MTases |
PANTHERi | PTHR32319:SF0, PTHR32319:SF0, 1 hit |
Pfami | View protein in Pfam PF01728, FtsJ, 1 hit PF01479, S4, 1 hit |
PIRSFi | PIRSF005578, TlyA, 1 hit |
SMARTi | View protein in SMART SM00363, S4, 1 hit |
SUPFAMi | SSF53335, SSF53335, 1 hit |
TIGRFAMsi | TIGR00478, tly, 1 hit |
PROSITEi | View protein in PROSITE PS50889, S4, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TLYA_MYCTU | |
Accessioni | P9WJ63Primary (citable) accession number: P9WJ63 Secondary accession number(s): L0TA51 Q7D847 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | December 2, 2020 | |
This is version 40 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families