RSMI_MYCTU
ID RSMI_MYCTU Reviewed; 285 AA.
AC P9WGW7; L0T856; O05588; P0A640;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 36.
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=Rv1003;
GN ORFNames=MTCI237.19;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION IN HUMAN MACROPHAGES.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16483748; DOI=10.1016/j.resmic.2005.10.007;
RA Cappelli G., Volpe E., Grassi M., Liseo B., Colizzi V., Mariani F.;
RT "Profiling of Mycobacterium tuberculosis gene expression during human
RT macrophage infection: upregulation of the alternative sigma factor G, a
RT group of transcriptional regulators, and proteins with unknown function.";
RL Res. Microbiol. 157:445-455(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- INDUCTION: Up-regulated 34-fold 7 days after infection of human
CC macrophages. {ECO:0000269|PubMed:16483748}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmI family.
CC {ECO:0000255|HAMAP-Rule:MF_01877}.
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DR EMBL; AL123456; CCP43753.1; -; Genomic_DNA.
DR PIR; F70602; F70602.
DR RefSeq; NP_215519.1; NC_000962.3.
DR RefSeq; WP_003405173.1; NZ_NVQJ01000018.1.
DR AlphaFoldDB; P9WGW7; -.
DR SMR; P9WGW7; -.
DR STRING; 83332.Rv1003; -.
DR PaxDb; P9WGW7; -.
DR DNASU; 887935; -.
DR GeneID; 45424975; -.
DR GeneID; 887935; -.
DR KEGG; mtu:Rv1003; -.
DR TubercuList; Rv1003; -.
DR eggNOG; COG0313; Bacteria.
DR OMA; RTMVFFE; -.
DR PhylomeDB; P9WGW7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..285
FT /note="Ribosomal RNA small subunit methyltransferase I"
FT /id="PRO_0000211946"
SQ SEQUENCE 285 AA; 29665 MW; 2F799A8057F64634 CRC64;
MSSGRLLLGA TPLGQPSDAS PRLAAALATA DVVAAEDTRR VRKLAKALDI RIGGRVVSLF
DRVEALRVTA LLDAINNGAT VLVVSDAGTP VISDPGYRLV AACIDAGVSV TCLPGPSAVT
TALVMSGLPA EKFCFEGFAP RKGAARRAWL AELAEERRTC VFFESPRRLA ACLNDAVEQL
GGARPAAICR ELTKVHEEVV RGSLDELAIW AAGGVLGEIT VVVAGAAPHA ELSSLIAQVE
EFVAAGIRVK DACSEVAAAH PGVRTRQLYD AVLQSRRETG GPAQP
