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Database: UniProt
Entry: A0A384KXW3_SHIFL
LinkDB: A0A384KXW3_SHIFL
Original site: A0A384KXW3_SHIFL 
ID   A0A384KXW3_SHIFL        Unreviewed;       286 AA.
AC   A0A384KXW3; A0A2S4N0T4; Q7BZR5; Q83JH0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=yraL {ECO:0000313|EMBL:AAN44654.1};
GN   Synonyms=rsmI {ECO:0000256|HAMAP-Rule:MF_01877};
GN   OrderedLocusNames=SF3187 {ECO:0000313|EMBL:AAN44654.1};
OS   Shigella flexneri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623 {ECO:0000313|EMBL:AAN44654.1, ECO:0000313|Proteomes:UP000001006};
RN   [1] {ECO:0000313|EMBL:AAN44654.1, ECO:0000313|Proteomes:UP000001006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a {ECO:0000313|Proteomes:UP000001006};
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
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; AE005674; AAN44654.1; -; Genomic_DNA.
DR   RefSeq; NP_708947.1; NC_004337.2.
DR   RefSeq; WP_000809275.1; NZ_WPGW01000004.1.
DR   AlphaFoldDB; A0A384KXW3; -.
DR   PaxDb; 198214-SF3187; -.
DR   GeneID; 1027135; -.
DR   KEGG; sfl:SF3187; -.
DR   PATRIC; fig|198214.7.peg.3786; -.
DR   OMA; HMHNEHK; -.
DR   Proteomes; UP000001006; 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:UP000001006};
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          14..213
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   286 AA;  31378 MW;  89DEA49EF48FB959 CRC64;
     MKQHQSADNS QGQLYIVPTP IGNLADITQR TLEVLQAVDL IAAEDTRHTG LLLQHFGINA
     RLFALHDHNE QQKAETLLAK LQEGQNIALV SDAGTPLIND PGYHLVRTCR EAGIRVVPLP
     GPCAAITALS AAGLPSDRFC YEGFLPAKSK GRRDALKAIE AEPRTLIFYE STHRLLDSLE
     DIVAVLGESR YVVLARELTK TWETIHGAPV GELLAWVKED ENRRKGEMVL IVEGHKAQEE
     DLPADALRTL ALLQAELPLK KAAALAAEIH GVKKNALYKY ALEQQG
//
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