ID L0M1C0_ENTBF Unreviewed; 429 AA.
AC L0M1C0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000256|HAMAP-Rule:MF_01856};
DE EC=2.1.1.176 {ECO:0000256|HAMAP-Rule:MF_01856};
DE AltName: Full=16S rRNA m5C967 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01856};
DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB {ECO:0000256|HAMAP-Rule:MF_01856};
GN Name=rsmB {ECO:0000256|HAMAP-Rule:MF_01856};
GN Synonyms=sun {ECO:0000256|HAMAP-Rule:MF_01856};
GN OrderedLocusNames=D782_0412 {ECO:0000313|EMBL:AGB76481.1};
OS Enterobacteriaceae bacterium (strain FGI 57).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=693444 {ECO:0000313|EMBL:AGB76481.1, ECO:0000313|Proteomes:UP000011002};
RN [1] {ECO:0000313|EMBL:AGB76481.1, ECO:0000313|Proteomes:UP000011002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI 57 {ECO:0000313|EMBL:AGB76481.1,
RC ECO:0000313|Proteomes:UP000011002};
RX PubMed=23469353; DOI=10.1128/genomeA.00238-12;
RA Aylward F.O., Tremmel D.M., Bruce D.C., Chain P., Chen A.,
RA Walston Davenport K., Detter C., Han C.S., Han J., Huntemann M.,
RA Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M.,
RA Pagani I., Pati A., Pitluck S., Deshpande S., Goodwin L., Woyke T.,
RA Currie C.R.;
RT "Complete genome of Enterobacteriaceae bacterium strain FGI 57, a strain
RT associated with leaf-cutter ant fungus gardens.";
RL Genome Announc. 1:E00238-12(2013).
CC -!- FUNCTION: Specifically methylates the cytosine at position 967 (m5C967)
CC of 16S rRNA. {ECO:0000256|ARBA:ARBA00002724, ECO:0000256|HAMAP-
CC Rule:MF_01856}.
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:0000256|ARBA:ARBA00000588, ECO:0000256|HAMAP-
CC Rule:MF_01856};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01856}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC ECO:0000256|HAMAP-Rule:MF_01856, ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR EMBL; CP003938; AGB76481.1; -; Genomic_DNA.
DR AlphaFoldDB; L0M1C0; -.
DR STRING; 693444.D782_0412; -.
DR KEGG; ebf:D782_0412; -.
DR PATRIC; fig|693444.3.peg.405; -.
DR eggNOG; COG0144; Bacteria.
DR eggNOG; COG0781; Bacteria.
DR HOGENOM; CLU_005316_0_4_6; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000011002; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016434; F:rRNA (cytosine) methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd00620; Methyltransferase_Sun; 1.
DR Gene3D; 1.10.287.730; Helix hairpin bin; 1.
DR Gene3D; 1.10.940.10; NusB-like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01856; 16SrRNA_methyltr_B; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
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; IPR023541; rRNA_ssu_MeTfrase_B_ent.
DR InterPro; IPR048019; RsmB-like_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00563; rsmB; 1.
DR PANTHER; PTHR22807:SF61; NOL1_NOP2_SUN FAMILY PROTEIN _ ANTITERMINATION NUSB DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF01029; NusB; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF48013; NusB-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01856};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01856}; Reference proteome {ECO:0000313|Proteomes:UP000011002};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01856};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_01856};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01856};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01856}.
FT DOMAIN 164..429
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 398..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 375
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01856,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 254..260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01856,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 277
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01856,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 303
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01856,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 322
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01856,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 429 AA; 48286 MW; 70E74014A28F0068 CRC64;
MKKNINLRSL AAQTVEQVVE QGQSLSNVLP AMQQKVSDKD KALLQELCFG VLRTLSQLEW
FIHKLMSRPM TGKQRTVHYL IMVGIYQLLY TRIPAHAALA ETVEGAIAIK RQQLKGLING
VLRQFQRQQD ELLAEFAQTE VRYLHPSWLV KRIKKAYPQQ WEAILEANNQ RPPMWLRVNR
NHHTRDAWLA LLTEAGLTGF PHADYPDAVR LETPAPVHAL PGFDEGWVTV QDASAQGCMT
YLQPENGEQI LDLCAAPGGK TTHILEVAPE ANVMAVDVDE KRLSRVYDNL KRLGMKATVK
QGDGRFPEQW CGEQQFDRIL LDAPCSATGV VRRHPDIKWL RRDRDIPELA QLQAEILNAT
WAHLKPGGTL VYATCSILPE ENSEQIAAFL QRTPDAVLSE TGTPEQPGKQ NLPGAEEGDG
FFYAKLIKK
//
