ID   B2HDL2_MYCMM            Unreviewed;       284 AA.
AC   B2HDL2;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   02-SEP-2026, entry version 79.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase I {ECO:0000256|HAMAP-Rule:MF_01877};
DE            EC=2.1.1.198 {ECO:0000256|HAMAP-Rule:MF_01877};
DE   AltName: Full=16S rRNA 2'-O-ribose C1402 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01877};
DE   AltName: Full=rRNA (cytidine-2'-O-)-methyltransferase RsmI {ECO:0000256|HAMAP-Rule:MF_01877};
GN   Name=rsmI {ECO:0000256|HAMAP-Rule:MF_01877};
GN   OrderedLocusNames=MMAR_4490 {ECO:0000313|EMBL:ACC42896.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC42896.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC42896.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
CC   -!- FUNCTION: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402
CC       (C1402) in 16S rRNA. {ECO:0000256|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 + S-adenosyl-L-homocysteine + H(+);
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:0000256|HAMAP-Rule:MF_01877};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01877}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmI family.
CC       {ECO:0000256|HAMAP-Rule:MF_01877}.
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DR   EMBL; CP000854; ACC42896.1; -; Genomic_DNA.
DR   RefSeq; WP_012396042.1; NC_010612.1.
DR   AlphaFoldDB; B2HDL2; -.
DR   STRING; 216594.MMAR_4490; -.
DR   KEGG; mmi:MMAR_4490; -.
DR   eggNOG; COG0313; Bacteria.
DR   HOGENOM; CLU_044779_0_0_11; -.
DR   OrthoDB; 9809084at2; -.
DR   Proteomes; UP000001190; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070677; F:rRNA (cytosine-2'-O-ribose)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031167; P:rRNA methylation; IEA:UniProtKB-UniRule.
DR   CDD; cd11648; RsmI; 1.
DR   FunFam; 3.30.950.10:FF:000002; Ribosomal RNA small subunit methyltransferase I; 1.
DR   FunFam; 3.40.1010.10:FF:000007; Ribosomal RNA small subunit methyltransferase I; 1.
DR   Gene3D; 3.40.1010.10; Cobalt-precorrin-4 Transmethylase, Domain 1; 1.
DR   Gene3D; 3.30.950.10; Methyltransferase, Cobalt-precorrin-4 Transmethylase, Domain 2; 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   NCBIfam; TIGR00096; 16S rRNA (cytidine(1402)-2'-O)-methyltransferase; 1.
DR   PANTHER; PTHR46111; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE I; 1.
DR   PANTHER; PTHR46111:SF1; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE I; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF005917; MTase_YraL; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR   PROSITE; PS01296; RSMI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01877};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01877}; Reference proteome {ECO:0000313|Proteomes:UP000001190};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_01877};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01877};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01877}.
FT   DOMAIN          11..208
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   284 AA;  29705 MW;  B78329B8708CA1DC CRC64;
     MTVGRLLLGA TPLGQPSDAS ARLIDALTSA DVVAAEDTRR VRTLAKALDI SIGGRVVSLF
     DRVEALRVGS LVEAIEAGAT VLVVSDAGMP VINDPGYRLV AACIEAGISV TCLPGPSAVT
     TALVVSGLAS DKFCFEGFAP RKSGARRAWL ASLAEEPRTC VFFESPRRLA ACLRDAVEQL
     GGSRPAAVCR ELTKVHEEVR RGSLGELADW AADGVLGEIT VVLAGAAPLH VDLQSLVAEV
     ENLVAAGIRV KDACSEVATG HQGIRTRELY DAVQLARRET DTAP
//