RSMB_BACSU
ID RSMB_BACSU Reviewed; 447 AA.
AC P94464;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Probable ribosomal RNA small subunit methyltransferase B {ECO:0000305};
DE EC=2.1.1.176 {ECO:0000250|UniProtKB:P36929};
DE AltName: Full=16S rRNA m5C967 methyltransferase {ECO:0000250|UniProtKB:P36929};
DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB {ECO:0000250|UniProtKB:P36929};
GN Name=rsmB {ECO:0000312|EMBL:CAB13447.1}; Synonyms=sun, yloM;
GN OrderedLocusNames=BSU15740;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9534248; DOI=10.1099/00221287-144-3-801;
RA Foulger D., Errington J.;
RT "A 28 kbp segment from the spoVM region of the Bacillus subtilis 168
RT genome.";
RL Microbiology 144:801-805(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-240.
RC STRAIN=168;
RX PubMed=9086272; DOI=10.1006/jmbi.1996.0835;
RA Mazel D., Coic E., Blanchard S., Saurin W., Marliere P.;
RT "A survey of polypeptide deformylase function throughout the eubacterial
RT lineage.";
RL J. Mol. Biol. 266:939-949(1997).
CC -!- FUNCTION: Specifically methylates the cytosine at position 967 (m5C967)
CC of 16S rRNA. {ECO:0000250|UniProtKB:P36929}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42748, Rhea:RHEA-COMP:10219, Rhea:RHEA-COMP:10220,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.176;
CC Evidence={ECO:0000250|UniProtKB:P36929};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P36929}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
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DR EMBL; Y13937; CAA74264.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13447.1; -; Genomic_DNA.
DR EMBL; Y10304; CAA71351.1; -; Genomic_DNA.
DR PIR; E69878; E69878.
DR RefSeq; NP_389456.1; NC_000964.3.
DR RefSeq; WP_003232068.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P94464; -.
DR SMR; P94464; -.
DR STRING; 224308.BSU15740; -.
DR PaxDb; P94464; -.
DR PRIDE; P94464; -.
DR EnsemblBacteria; CAB13447; CAB13447; BSU_15740.
DR GeneID; 938106; -.
DR KEGG; bsu:BSU15740; -.
DR PATRIC; fig|224308.179.peg.1714; -.
DR eggNOG; COG0144; Bacteria.
DR eggNOG; COG0781; Bacteria.
DR InParanoid; P94464; -.
DR OMA; RVNRQHH; -.
DR PhylomeDB; P94464; -.
DR BioCyc; BSUB:BSU15740-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR Gene3D; 1.10.940.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR035926; NusB-like_sf.
DR InterPro; IPR006027; NusB_RsmB_TIM44.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR004573; rRNA_ssu_MeTfrase_B.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807; PTHR22807; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF01029; NusB; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF48013; SSF48013; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00563; rsmB; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..447
FT /note="Probable ribosomal RNA small subunit
FT methyltransferase B"
FT /id="PRO_0000211815"
FT ACT_SITE 382
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 259..265
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 310
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 329
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 447 AA; 50274 MW; 85AC153408CE9F4F CRC64;
MKKTSVRDIA LEALIKLEQN QAYSNLLLKS VIKSNELSDQ NRGLLTELVY GTLQNKIALD
YMLKPFINKP QKVKPWVIQL LRLSLYQMEY LEKIPDRAAI HEAVEIAKIR GHKGIASFVN
GVLRSIQREG VPSFDAIEDP VRRLATETSH PEWLVKEWAD AYGFEAAEKI CRIHLIPPKQ
TLRVNQMKAD RAELLDQMAA EGIEVEKGDL AEDAVKLLKG TIAGTHFFQN GEVSIQDESS
MLVARALDPK SDETVLDACA APGGKSAHIA ELMKNKGSVT SLDLHKHKVK LIKEAADRLG
LTIIHAETMD ARKAGETFEN EQFDRILVDA PCSGFGVIRR KPDMKYTKKP DDSARLAEIQ
LSILREIAPL VKKGGTLVYS TCTMDRTEND EVIHAFIQEH PDFEPDLSLE KRLPEKVRPF
VRDGRLQILP HYFGTDGFFI CSMRKKG
