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Database: UniProt
Entry: F5X2S6_STRPX
LinkDB: F5X2S6_STRPX
Original site: F5X2S6_STRPX 
ID   F5X2S6_STRPX            Unreviewed;       288 AA.
AC   F5X2S6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
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=SGPB_1560 {ECO:0000313|EMBL:BAK30585.1};
OS   Streptococcus pasteurianus (strain ATCC 43144 / JCM 5346 / CDC 1723-81).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=981540 {ECO:0000313|EMBL:BAK30585.1, ECO:0000313|Proteomes:UP000007946};
RN   [1] {ECO:0000313|EMBL:BAK30585.1, ECO:0000313|Proteomes:UP000007946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43144 / JCM 5346 / CDC 1723-81
RC   {ECO:0000313|Proteomes:UP000007946};
RX   PubMed=21633709; DOI=10.1371/journal.pone.0020519;
RA   Lin I.-H., Liu T.-T., Teng Y.-T., Wu H.-L., Liu Y.-M., Wu K.-M.,
RA   Chang C.-H., Hsu M.-T.;
RT   "Sequencing and comparative genome analysis of two pathogenic Streptococcus
RT   gallolyticus subspecies: genome plasticity, adaptation and virulence.";
RL   PLoS ONE 6:E20519-E20519(2011).
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 + 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: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; AP012054; BAK30585.1; -; Genomic_DNA.
DR   RefSeq; WP_003066004.1; NC_015600.1.
DR   AlphaFoldDB; F5X2S6; -.
DR   STRING; 981540.SGPB_1560; -.
DR   GeneID; 76468487; -.
DR   KEGG; stb:SGPB_1560; -.
DR   HOGENOM; CLU_044779_1_0_9; -.
DR   Proteomes; UP000007946; 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   CDD; cd11648; RsmI; 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:UP000007946};
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          16..214
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   288 AA;  32211 MW;  9829BA7139E425C8 CRC64;
     MKVQKSFKNQ TTYGQLYLVP TPIGNMQDMT YRAVEILKNA DFVCAEDTRN TGLLLKHFDI
     SAKQISFHEH NAYEKIPELI ALMKEGKILA QVSDAGMPSI SDPGHDLVKA AIAEEITVVA
     IPGASAGITA LIASGLAPQP HIFYGFLPRK AKQQKEFFEA KKQYPETQIF YESPYRVADT
     LDNMLAVYGD RKIVLVRELT KLFEEYQRGC ISEILEYIAQ NPLKGECLIV VSGQDEIATL
     EEISENINPA ELVAQLIEAG DKPNQAIKKI AKTYGLNRQE VYNAYHQL
//
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