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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}.
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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
 
 
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