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RLMB_VIBPA
ID   RLMB_VIBPA              Reviewed;         247 AA.
AC   Q87L11;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=23S rRNA (guanosine-2'-O-)-methyltransferase RlmB {ECO:0000255|HAMAP-Rule:MF_01887};
DE            EC=2.1.1.185 {ECO:0000255|HAMAP-Rule:MF_01887};
DE   AltName: Full=23S rRNA (guanosine2251 2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01887};
DE   AltName: Full=23S rRNA Gm2251 2'-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01887};
GN   Name=rlmB {ECO:0000255|HAMAP-Rule:MF_01887}; OrderedLocusNames=VP2806;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
CC   -!- FUNCTION: Specifically methylates the ribose of guanosine 2251 in 23S
CC       rRNA. {ECO:0000255|HAMAP-Rule:MF_01887}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(2251) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-
CC         methylguanosine(2251) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:24140, Rhea:RHEA-COMP:10239, Rhea:RHEA-COMP:10241,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74445; EC=2.1.1.185;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01887};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01887}.
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase TrmH family. RlmB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01887}.
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DR   EMBL; BA000031; BAC61069.1; -; Genomic_DNA.
DR   RefSeq; NP_799185.1; NC_004603.1.
DR   RefSeq; WP_005480034.1; NC_004603.1.
DR   AlphaFoldDB; Q87L11; -.
DR   SMR; Q87L11; -.
DR   STRING; 223926.28807816; -.
DR   EnsemblBacteria; BAC61069; BAC61069; BAC61069.
DR   GeneID; 1190356; -.
DR   KEGG; vpa:VP2806; -.
DR   PATRIC; fig|223926.6.peg.2698; -.
DR   eggNOG; COG0566; Bacteria.
DR   HOGENOM; CLU_021322_0_1_6; -.
DR   OMA; QVPPYEY; -.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   HAMAP; MF_01887; 23SrRNA_methyltr_B; 1.
DR   InterPro; IPR024915; 23S_rRNA_MeTrfase_RlmB.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR029064; L30e-like.
DR   InterPro; IPR004441; rRNA_MeTrfase_TrmH.
DR   InterPro; IPR001537; SpoU_MeTrfase.
DR   InterPro; IPR013123; SpoU_subst-bd.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   PANTHER; PTHR46429; PTHR46429; 1.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   Pfam; PF08032; SpoU_sub_bind; 1.
DR   SMART; SM00967; SpoU_sub_bind; 1.
DR   SUPFAM; SSF55315; SSF55315; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
DR   TIGRFAMs; TIGR00186; rRNA_methyl_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..247
FT                   /note="23S rRNA (guanosine-2'-O-)-methyltransferase RlmB"
FT                   /id="PRO_0000159806"
FT   BINDING         197
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01887"
FT   BINDING         217
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01887"
FT   BINDING         226
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01887"
SQ   SEQUENCE   247 AA;  26715 MW;  D39255232A28FEFE CRC64;
     MSNEFIYGIH AVKAVLEREP ERFIEAYVLK GRQDDRLMPI LNDLQVCGVS IQQMTRKTLD
     DKAHGANHQG IIARVKVAKQ LNENDIDDIL AQHETPLLLV LDGVTDPHNL GACLRNADAA
     GVAAIIVPKD RSAPMNATVS KVACGAAEVV PLIRVTNLAR TMRTLQEQGI WFVGTAGEAT
     HDIYQAKLTG PLAIVMGAEG DGMRRLTRET CDDLIKIPMA GSVSSLNVSV ASGICLFEAV
     RQRLAAK
 
 
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