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⊟Summary[edit | edit source]
- pan ID?: SAUPAN002225000
- symbol?: rsmI
- synonym:
- description?: rRNA (cytidine-2'-O-)-methyltransferase
- rRNA (cytidine-2'-O-)-methyltransferase
- 16S rRNA (cytidine(1402)-2'-O)-methyltransferase
- tetrapyrrole methylase
- tetrapyrrole methylase family protein
- tetrapyrrole (corrin/porphyrin) methylase family protein
- rRNA small subunit methyltransferase I
- tetrapyrrole (Corrin/Porphyrin) Methylases family protein
- tetrapyrrole (corrin/porphyrin) methyltransferase
- Tetrapyrrole (Corrin-Porphyrin) methylase family protein UPF0011
- uroporphyrin-III C/tetrapyrrole (Corrin/Porphyrin) methyltransferase
- uroporphyrin-III C/tetrapyrrole methyltransferase
descriptions from strain specific annotations:
- strand?: +
- coordinates?: 2735263..2736102
- synteny block?: BlockID0015240
- occurrence?: in 100% of 34 strains
rsmI : ribosome small subunit and tRNA methyltransferase I [1]
Ribosome small subunit methyltransferase I (alt: ribosome small subunit ribose methyltransferase I, 16S rRNA 4-methylcytosine (1412)-O-(2')-methyltransferase) attaches a methyl group to the ribose sugar 2'-position of 4-methylcytosine residue 1412 in 16S ribosomal RNA (S. aureus numbering; 4-methylcytosine 1402 by E. coli numbering). This only occurs after RsmH-mediated conversion of cytosine to 4-methylcytosine. RsmI is a dual-function enzyme and is also able to attach a methyl group to the ribose sugar 2'-position of cytosine nucleobases at the anticodon loop-proximal residue 34 of transfer RNAs such as tRNALCAA.
- 16S rRNA : m4C (1412) → m4Cm (1412)
- tRNA : C (34) → Cm (34)
⊟Orthologs[edit | edit source]
04-02981:
SA2981_0464
08BA02176:
C248_0543
11819-97:
MS7_0466
6850:
RSAU_000426
71193:
ST398NM01_0555
ECT-R 2:
ECTR2_429
ED133:
SAOV_0510
ED98:
SAAV_0435
HO 5096 0412:
SAEMRSA15_04150
JH1:
SaurJH1_0523
JH9:
SaurJH9_0510
JKD6008:
SAA6008_00493
JKD6159:
SAA6159_00440
JSNZ:
JSNZ_000428 (rsmI)
LGA251:
SARLGA251_04230
M013:
M013TW_0458
MRSA252:
SAR0490
MSHR1132:
SAMSHR1132_04330
MSSA476:
SAS0446
Mu3:
SAHV_0486
Mu50:
SAV0489
MW2:
MW0444
RF122:
SAB0438
ST398:
SAPIG0555
T0131:
SAT0131_00534
TCH60:
HMPREF0772_10032
TW20:
SATW20_05570
USA300_TCH1516:
USA300HOU_0489
VC40:
SAVC_02030
⊟Genome Viewer[edit | edit source]
| COL | |
| N315 | |
| NCTC8325 | |
| Newman | |
| USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL MAVLYLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPTPLKSYHEHNK
N315 MAVLYLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPTPLKSYHEHNK
NCTC8325 MAVLYLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPTPLKSYHEHNK
Newman MAVLYLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPTPLKSYHEHNK
USA300_FPR3757 MAVLYLVGTPIGNLADITYRAVDVLKRVDMIACEDTRVTSKLCNHYDIPTPLKSYHEHNK
************************************************************
COL DKQTAFIIEQLELGLDVALVSDAGLPLISDPGYELVVAAREANIKVETVPGPNAGLTALM
N315 DKQTAFIIEQLELGLDVALVSDAGLPLISDPGYELVVAAREANIKVETVPGPNAGLTALM
NCTC8325 DKQTAFIIEQLELGLDVALVSDAGLPLISDPGYELVVAAREANIKVETVPGPNAGLTALM
Newman DKQTAFIIEQLELGLDVALVSDAGLPLISDPGYELVVAAREANIKVETVPGPNAGLTALM
USA300_FPR3757 DKQTAFIIEQLELGLDVALVSDAGLPLISDPGYELVVAAREANIKVETVPGPNAGLTALM
************************************************************
COL ASGLPSYVYTFLGFLPRKEKEKSAVLEQRMHENSTLIIYESPHRVTDTLKTIAKIDATRQ
N315 ASGLPSYVYTFLGFLPRKEKEKSAVLEQRMHENSTLIIYESPHRVTDTLKTIAKIDATRQ
NCTC8325 ASGLPSYVYTFLGFLPRKEKEKSAVLEQRMHENSTLIIYESPHRVTDTLKTIAKIDATRQ
Newman ASGLPSYVYTFLGFLPRKEKEKSAVLEQRMHENSTLIIYESPHRVTDTLKTIAKIDATRQ
USA300_FPR3757 ASGLPSYVYTFLGFLPRKEKEKSAVLEQRMHENSTLIIYESPHRVTDTLKTIAKIDATRQ
************************************************************
COL VSLGRELTKKFEQIVTDDVTQLQALIQQGDVPLKGEFVILIEGAKANNEISWFDDLSINE
N315 VSLGRELTKKFEQIVTDDVTQLQALIQQGDVPLKGEFVILIEGAKANNEISWFDDLSINE
NCTC8325 VSLGRELTKKFEQIVTDDVTQLQALIQQGDVPLKGEFVILIEGAKANNEISWFDDLSINE
Newman VSLGRELTKKFEQIVTDDVTQLQALIQQGDVPLKGEFVILIEGAKANNEISWFDDLSINE
USA300_FPR3757 VSLGRELTKKFEQIVTDDVTQLQALIQQGDVPLKGEFVILIEGAKANNEISWFDDLSINE
************************************************************
COL HVDHYIQTSQMKPKQAIKKVAEERQLKTNEVYNIYHQIS
N315 HVDHYIQTSQMKPKQAIKKVAEERQLKTNEVYNIYHQIS
NCTC8325 HVDHYIQTSQMKPKQAIKKVAEERQLKTNEVYNIYHQIS
Newman HVDHYIQTSQMKPKQAIKKVAEERQLKTNEVYNIYHQIS
USA300_FPR3757 HVDHYIQTSQMKPKQAIKKVAEERQLKTNEVYNIYHQIS
***************************************
- ↑ Tatsuhiko Kyuma, Satoshi Kimura, Yuichi Hanada, Tsutomu Suzuki, Kazuhisa Sekimizu, Chikara Kaito
Ribosomal RNA methyltransferases contribute to Staphylococcus aureus virulence.
FEBS J: 2015, 282(13);2570-84
[PubMed:25893373] [WorldCat.org] [DOI] (I p)Alexander Golubev, Bulat Fatkhullin, Iskander Khusainov, Lasse Jenner, Azat Gabdulkhakov, Shamil Validov, Gulnara Yusupova, Marat Yusupov, Konstantin Usachev
Cryo-EM structure of the ribosome functional complex of the human pathogen Staphylococcus aureus at 3.2 Å resolution.
FEBS Lett: 2020, 594(21);3551-3567
[PubMed:32852796] [WorldCat.org] [DOI] (I p)Adrián González-López, Daniel S D Larsson, Ravi Kiran Koripella, Brett N Cain, Martin Garcia Chavez, Paul J Hergenrother, Suparna Sanyal, Maria Selmer
Structures of the Staphylococcus aureus ribosome inhibited by fusidic acid and fusidic acid cyclopentane.
Sci Rep: 2024, 14(1);14253
[PubMed:38902339] [WorldCat.org] [DOI] (I e)