TLYA_CAMJJ
ID TLYA_CAMJJ Reviewed; 253 AA.
AC A0A0H3PEK7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=23S rRNA (cytidine-2'-O)-methyltransferase TlyA {ECO:0000303|PubMed:29404277};
DE EC=2.1.1.226 {ECO:0000269|PubMed:24796671, ECO:0000269|PubMed:29404277};
DE AltName: Full=23S rRNA (cytidine1920-2'-O)-methyltransferase {ECO:0000303|PubMed:29404277};
DE AltName: Full=Hemolysin A {ECO:0000312|EMBL:EAQ73153.1};
GN Name=tlyA {ECO:0000303|PubMed:24796671, ECO:0000303|PubMed:29404277,
GN ECO:0000303|PubMed:32134554, ECO:0000312|EMBL:EAQ73153.1};
GN OrderedLocusNames=CJJ81176_0616 {ECO:0000312|EMBL:EAQ73153.1};
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242 {ECO:0000312|EMBL:EAQ73153.1};
RN [1] {ECO:0000312|Proteomes:UP000000646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176 {ECO:0000312|Proteomes:UP000000646};
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=81-176 {ECO:0000303|PubMed:18389311};
RX PubMed=18389311; DOI=10.1007/s00284-008-9130-z;
RA Salamaszynska-Guz A., Klimuszko D.;
RT "Functional analysis of the Campylobacter jejuni cj0183 and cj0588 genes.";
RL Curr. Microbiol. 56:592-596(2008).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=81-176 {ECO:0000303|PubMed:23971210};
RX PubMed=23971210; DOI=10.2478/pjvs-2013-0053;
RA Salamaszynska-Guz A., Godlewski M.M., Klimuszko D.;
RT "Influence of mutation in cj0183 and cj0588 genes for colonization
RT abilities of Campylobacter jejuni in Caco-2 cells using confocal laser
RT scanning microscope.";
RL Pol. J. Vet. Sci. 16:387-389(2013).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, AND 3D-STRUCTURE MODELING.
RC STRAIN=81-176 {ECO:0000303|PubMed:24796671};
RX PubMed=24796671; DOI=10.1016/j.bbrc.2014.04.104;
RA Salamaszynska-Guz A., Taciak B., Kwiatek A., Klimuszko D.;
RT "The Cj0588 protein is a Campylobacter jejuni RNA methyltransferase.";
RL Biochem. Biophys. Res. Commun. 448:298-302(2014).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-80;
RP ASP-162 AND LYS-188, AND 3D-STRUCTURE MODELING OF THE CATALYTIC DOMAIN.
RC STRAIN=81-176 {ECO:0000303|PubMed:29404277};
RX PubMed=29404277; DOI=10.3389/fcimb.2017.00533;
RA Salamaszynska-Guz A., Rose S., Lykkebo C.A., Taciak B., Bacal P.,
RA Uspienski T., Douthwaite S.;
RT "Biofilm Formation and Motility Are Promoted by Cj0588-Directed Methylation
RT of rRNA in Campylobacter jejuni.";
RL Front. Cell. Infect. Microbiol. 7:533-533(2017).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-188.
RC STRAIN=81-176 {ECO:0000303|PubMed:32134554};
RX PubMed=32134554; DOI=10.1111/cmi.13199;
RA Salamaszynska-Guz A., Serafinska I., Bacal P., Douthwaite S.;
RT "Virulence properties of Campylobacter jejuni are enhanced by displaying a
RT mycobacterial TlyA methylation pattern in its rRNA.";
RL Cell. Microbiol. 22:e13199-e13199(2020).
CC -!- FUNCTION: Catalyzes the 2'-O-methylation at nucleotide C1920 in 23S
CC rRNA (PubMed:24796671, PubMed:29404277). Enhances motility
CC (PubMed:24796671, PubMed:29404277, PubMed:32134554). Enchances biofilm
CC formation (PubMed:29404277, PubMed:32134554). Involved in the assembly
CC of 70S ribosomes (PubMed:24796671). Involved in virulence by promoting
CC adherence and invasion to host cells (PubMed:18389311, PubMed:23971210,
CC PubMed:32134554). Involved in pathogenicity by modulating secretion of
CC host-protective chemokine interleukin 8 (IL-8) (PubMed:32134554).
CC Involved in susceptibility to antibiotic capreomycin (PubMed:24796671,
CC PubMed:32134554). {ECO:0000269|PubMed:18389311,
CC ECO:0000269|PubMed:23971210, ECO:0000269|PubMed:24796671,
CC ECO:0000269|PubMed:29404277, ECO:0000269|PubMed:32134554}.
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:0000269|PubMed:24796671, ECO:0000269|PubMed:29404277};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43201;
CC Evidence={ECO:0000269|PubMed:24796671, ECO:0000269|PubMed:29404277};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.8 uM for 50S ribosomal subunit (at pH 7.5 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:24796671};
CC KM=5.8 uM for S-adenosyl-L-methionine (at pH 7.5 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:24796671};
CC Note=kcat is 0.0048 min(-1) for 50S ribosomal subunit. kcat is 0.0044
CC min(-1) for S-adenosyl-L-methionine. {ECO:0000269|PubMed:24796671};
CC Temperature dependence:
CC High methylation activity of the 50S ribosomal subunit at 37 degrees
CC Celsius. Loss of activity at 42 degrees Celsius.
CC {ECO:0000269|PubMed:24796671};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have no 2'-O-methylation
CC activity at nucleotide C1920 in 23S rRNA (PubMed:29404277). Impeded
CC motility (PubMed:24796671, PubMed:29404277, PubMed:32134554). Impaired
CC biofilm formation (PubMed:29404277, PubMed:32134554). Cells form clumps
CC which lack the structural roughness seen in the wild-type. The cells
CC are less bulky, but otherwise they have no obvious alteration in
CC dimensions, shape or flagellar structure (PubMed:29404277).
CC Accumulation of 50S ribosomal subunits and reduced amount of functional
CC 70S ribosomes (PubMed:24796671). Reduced adherence to the surface of
CC Caco-2 human intestinal epithelial cells and impaired capacity to
CC invade them (PubMed:18389311, PubMed:23971210, PubMed:32134554).
CC Reduced interleukin 8 (IL-8) chemokine secretion by the Caco-2 cells.
CC Impaired adhesion and invasion to RAW264.7 murine macrophage cells, but
CC no effect on survival within the macrophages as both the wild-type and
CC mutant cells are killed within 48 hours (PubMed:32134554). Resistant to
CC capreomycin indicated by increased minimal inhibitory concentration
CC (MIC) value (PubMed:24796671, PubMed:32134554). No difference in
CC hemolytic activity between the mutant and the wild-type
CC (PubMed:18389311). {ECO:0000269|PubMed:18389311,
CC ECO:0000269|PubMed:23971210, ECO:0000269|PubMed:24796671,
CC ECO:0000269|PubMed:29404277, ECO:0000269|PubMed:32134554}.
CC -!- SIMILARITY: Belongs to the TlyA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000538; EAQ73153.1; -; Genomic_DNA.
DR RefSeq; WP_002868894.1; NC_008787.1.
DR STRING; 354242.CJJ81176_0616; -.
DR EnsemblBacteria; EAQ73153; EAQ73153; CJJ81176_0616.
DR KEGG; cjj:CJJ81176_0616; -.
DR eggNOG; COG1189; Bacteria.
DR HOGENOM; CLU_058015_1_0_7; -.
DR OMA; VLMVKPQ; -.
DR Proteomes; UP000000646; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0048870; P:cell motility; IMP:UniProtKB.
DR GO; GO:0071236; P:cellular response to antibiotic; IMP:UniProtKB.
DR GO; GO:0042256; P:mature ribosome assembly; IMP:UniProtKB.
DR GO; GO:0000451; P:rRNA 2'-O-methylation; IDA:UniProtKB.
DR GO; GO:0016032; P:viral process; IMP:UniProtKB.
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; 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 SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Transferase; Virulence.
FT CHAIN 1..253
FT /note="23S rRNA (cytidine-2'-O)-methyltransferase TlyA"
FT /id="PRO_0000454899"
FT DOMAIN 1..73
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT MUTAGEN 80
FT /note="K->A: Loss of 2'-O-methylation activity at
FT nucleotide C1920 in 23S rRNA. Reduced motility and impaired
FT biofilm formation."
FT /evidence="ECO:0000269|PubMed:29404277"
FT MUTAGEN 162
FT /note="D->A: Loss of 2'-O-methylation activity at
FT nucleotide C1920 in 23S rRNA. Reduced motility and impaired
FT biofilm formation."
FT /evidence="ECO:0000269|PubMed:29404277"
FT MUTAGEN 188
FT /note="K->A: Loss of 2'-O-methylation activity at
FT nucleotide C1920 in 23S rRNA. Reduced motility and impaired
FT biofilm formation. Reduced adherence to the surface of
FT Caco-2 human intestinal epithelial cells and impaired
FT capacity to invade them. Reduced interleukin 8 (IL-8)
FT chemokine secretion by the Caco-2 cells. Impaired adhesion
FT and invasion to RAW264.7 murine macrophage cells, but no
FT effect on survival rates within the macrophages. Increased
FT minimal inhibitory concentration (MIC) value for
FT capreomycin."
FT /evidence="ECO:0000269|PubMed:29404277,
FT ECO:0000269|PubMed:32134554"
SQ SEQUENCE 253 AA; 29175 MW; 2B6C5F93479B4E10 CRC64;
MRFDFFVSKR LNISRNKALE LIENEEVLLN GKSFKASFDV KNFLENLKKT QDLNPEDILL
TDGLKLDLLS EIYVSRAALK LKNFLEENGI EIKHKNCLDI GSSTGGFVQI LLENQALKIT
ALDVGNNQLH LSLRTNEKII LHENTDLRTF KSEEKFELIT CDVSFISLIN LLYYIDNLAL
KEIILLFKPQ FEVGKNIKRD KKGVLKDDKA ILKARMDFEK ACAKLGWLLK NTQKSSIKGK
EGNVEYFYYY IKN