RSMI_HELPY
ID RSMI_HELPY Reviewed; 287 AA.
AC P56204;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase I {ECO:0000255|HAMAP-Rule:MF_01877};
DE EC=2.1.1.198 {ECO:0000255|HAMAP-Rule:MF_01877};
DE AltName: Full=16S rRNA 2'-O-ribose C1402 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01877};
DE AltName: Full=rRNA (cytidine-2'-O-)-methyltransferase RsmI {ECO:0000255|HAMAP-Rule:MF_01877};
GN Name=rsmI {ECO:0000255|HAMAP-Rule:MF_01877}; OrderedLocusNames=HP_0552;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
CC -!- FUNCTION: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402
CC (C1402) in 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42924, Rhea:RHEA-COMP:10285, Rhea:RHEA-COMP:10286,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.198;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01877};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01877}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmI family.
CC {ECO:0000255|HAMAP-Rule:MF_01877}.
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DR EMBL; AE000511; AAD07618.1; -; Genomic_DNA.
DR PIR; H64588; H64588.
DR RefSeq; NP_207347.1; NC_000915.1.
DR RefSeq; WP_000965287.1; NC_018939.1.
DR AlphaFoldDB; P56204; -.
DR SMR; P56204; -.
DR DIP; DIP-3639N; -.
DR IntAct; P56204; 3.
DR MINT; P56204; -.
DR STRING; 85962.C694_02855; -.
DR PaxDb; P56204; -.
DR PRIDE; P56204; -.
DR EnsemblBacteria; AAD07618; AAD07618; HP_0552.
DR KEGG; hpy:HP_0552; -.
DR PATRIC; fig|85962.47.peg.597; -.
DR eggNOG; COG0313; Bacteria.
DR OMA; FIAFHSH; -.
DR PhylomeDB; P56204; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070677; F:rRNA (cytosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IBA:GO_Central.
DR CDD; cd11648; RsmI; 1.
DR Gene3D; 3.30.950.10; -; 1.
DR Gene3D; 3.40.1010.10; -; 1.
DR HAMAP; MF_01877; 16SrRNA_methyltr_I; 1.
DR InterPro; IPR000878; 4pyrrol_Mease.
DR InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR InterPro; IPR008189; rRNA_ssu_MeTfrase_I.
DR InterPro; IPR018063; SAM_MeTrfase_RsmI_CS.
DR PANTHER; PTHR46111; PTHR46111; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF005917; MTase_YraL; 1.
DR SUPFAM; SSF53790; SSF53790; 1.
DR TIGRFAMs; TIGR00096; TIGR00096; 1.
DR PROSITE; PS01296; RSMI; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..287
FT /note="Ribosomal RNA small subunit methyltransferase I"
FT /id="PRO_0000211941"
SQ SEQUENCE 287 AA; 32719 MW; 443F19E96159EFE9 CRC64;
MLYFLPTPIG NLADITLRAL EVLERCEVFL CEDTRVSKRL LHLLAQNPII SHSFPNIATK
KREFIAFHSH NDQEFLNQIK PSFFDKEIAV MSDAGMPSLS DPGMSLAAYA LKHNIQYDVL
PGANALTTAF CASGFLEGRF FYAGFLPHKS KERRLKIAKI LNALAYLEEK TPVVFYESPH
RLLETLKDLN DLAKGMHLFA AKELTKLHQQ YYLGEVSQII ERLQQSTIQG EWVLVLLNEK
KIEPCMGLSA LLELDLPPKI KAKIEAVMTQ KNAKELYFQR LLEEKNQ