TLYA_MYCTO
ID TLYA_MYCTO Reviewed; 268 AA.
AC P9WJ62; L0TA51; O07264; Q50760; Q79FL7; Q7D847;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=16S/23S rRNA (cytidine-2'-O)-methyltransferase TlyA;
DE EC=2.1.1.226 {ECO:0000250|UniProtKB:P9WJ63};
DE EC=2.1.1.227 {ECO:0000250|UniProtKB:P9WJ63};
DE AltName: Full=16S rRNA (cytidine1409-2'-O)-methyltransferase;
DE AltName: Full=23S rRNA (cytidine1920-2'-O)-methyltransferase;
DE AltName: Full=Hemolysin TlyA;
GN Name=tlyA; OrderedLocusNames=MT1733;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=15673735; DOI=10.1128/aac.49.2.571-577.2005;
RA Maus C.E., Plikaytis B.B., Shinnick T.M.;
RT "Mutation of tlyA confers capreomycin resistance in Mycobacterium
RT tuberculosis.";
RL Antimicrob. Agents Chemother. 49:571-577(2005).
CC -!- FUNCTION: Acts as a host evasion factor, that significantly contributes
CC to the pathogenesis of M.tuberculosis by modulating adaptive immune
CC responses by inhibiting host-protective Th1 and Th17 cytokine responses
CC as well as autophagy. Catalyzes the 2'-O-methylation at nucleotides
CC C1409 in 16S rRNA and C1920 in 23S rRNA. Is likely involved in
CC ribosomal biogenesis. Also exhibits hemolytic activity in vitro, by
CC binding with and oligomerizing into host cell membranes.
CC {ECO:0000250|UniProtKB:P9WJ63}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(1409) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(1409) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43204, Rhea:RHEA-COMP:10405, Rhea:RHEA-COMP:10406,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.227;
CC Evidence={ECO:0000250|UniProtKB:P9WJ63};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(1920) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(1920) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43200, Rhea:RHEA-COMP:10403, Rhea:RHEA-COMP:10404,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.226;
CC Evidence={ECO:0000250|UniProtKB:P9WJ63};
CC -!- SUBUNIT: Can form oligomers on macrophage phagosomal membranes.
CC {ECO:0000250|UniProtKB:P9WJ63}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WJ63}.
CC Secreted, cell wall {ECO:0000250|UniProtKB:P9WJ63}. Host cell membrane
CC {ECO:0000250|UniProtKB:P9WJ63}. Note=Can bind to target membranes such
CC as macrophage phagosomal membranes. In native and recombinant hosts
CC (M.smegmatis and E.coli), M.tuberculosis TlyA can reach the bacterial
CC surface in functional form and colocalizes with the HBHA protein which
CC is known to be part of cell-wall. TlyA does not seem to depend on
CC either Tat or Sec pathways for translocation to cell-wall. Appears to
CC be capable of reaching the extra-cellular milieu using a vesicle
CC mediated transport. {ECO:0000250|UniProtKB:P9WJ63}.
CC -!- DISRUPTION PHENOTYPE: Inactivation leads to capreomycin resistance.
CC {ECO:0000269|PubMed:15673735}.
CC -!- SIMILARITY: Belongs to the TlyA family. {ECO:0000305}.
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DR EMBL; AE000516; AAK46002.1; -; Genomic_DNA.
DR PIR; E70502; E70502.
DR RefSeq; WP_003408382.1; NZ_KK341227.1.
DR PDB; 5EOV; X-ray; 1.70 A; A=64-268.
DR PDBsum; 5EOV; -.
DR AlphaFoldDB; P9WJ62; -.
DR SMR; P9WJ62; -.
DR EnsemblBacteria; AAK46002; AAK46002; MT1733.
DR GeneID; 45425663; -.
DR KEGG; mtc:MT1733; -.
DR PATRIC; fig|83331.31.peg.1861; -.
DR HOGENOM; CLU_058015_1_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR004538; Haemolysin_A/TlyA.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR32319:SF0; PTHR32319:SF0; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF01479; S4; 1.
DR PIRSF; PIRSF005578; TlyA; 1.
DR SMART; SM00363; S4; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00478; tly; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Cytolysis; Cytoplasm; Hemolysis;
KW Host cell membrane; Host membrane; Membrane; Methyltransferase;
KW Ribosome biogenesis; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Secreted; Toxin; Transferase; Virulence.
FT CHAIN 1..268
FT /note="16S/23S rRNA (cytidine-2'-O)-methyltransferase TlyA"
FT /id="PRO_0000427885"
FT DOMAIN 5..67
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:5EOV"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:5EOV"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5EOV"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:5EOV"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:5EOV"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:5EOV"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:5EOV"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:5EOV"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:5EOV"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:5EOV"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:5EOV"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:5EOV"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:5EOV"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:5EOV"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:5EOV"
FT HELIX 201..217
FT /evidence="ECO:0007829|PDB:5EOV"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:5EOV"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:5EOV"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:5EOV"
SQ SEQUENCE 268 AA; 28074 MW; B62AB8400CCC71CE CRC64;
MARRARVDAE LVRRGLARSR QQAAELIGAG KVRIDGLPAV KPATAVSDTT ALTVVTDSER
AWVSRGAHKL VGALEAFAIA VAGRRCLDAG ASTGGFTEVL LDRGAAHVVA ADVGYGQLAW
SLRNDPRVVV LERTNARGLT PEAIGGRVDL VVADLSFISL ATVLPALVGC ASRDADIVPL
VKPQFEVGKG QVGPGGVVHD PQLRARSVLA VARRAQELGW HSVGVKASPL PGPSGNVEYF
LWLRTQTDRA LSAKGLEDAV HRAISEGP
