ID A0A172QAM2_9STRE Unreviewed; 440 AA.
AC A0A172QAM2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=16S rRNA (cytosine(967)-C(5))-methyltransferase {ECO:0000256|ARBA:ARBA00012140};
DE EC=2.1.1.176 {ECO:0000256|ARBA:ARBA00012140};
DE AltName: Full=16S rRNA m5C967 methyltransferase {ECO:0000256|ARBA:ARBA00030399};
DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB {ECO:0000256|ARBA:ARBA00031088};
GN ORFNames=A0O21_07215 {ECO:0000313|EMBL:AND80467.1};
OS Streptococcus pantholopis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1811193 {ECO:0000313|EMBL:AND80467.1, ECO:0000313|Proteomes:UP000077317};
RN [1] {ECO:0000313|EMBL:AND80467.1, ECO:0000313|Proteomes:UP000077317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA 26 {ECO:0000313|EMBL:AND80467.1,
RC ECO:0000313|Proteomes:UP000077317};
RX PubMed=27226124; DOI=10.1099/ijsem.0.001189;
RA Bai X., Xiong Y., Lu S., Jin D., Lai X., Yang J., Niu L., Hu S., Meng X.,
RA Pu J., Ye C., Xu J.;
RT "Streptococcuspantholopis sp. nov., isolated from faeces of the Tibetan
RT antelope (Pantholops hodgsonii).";
RL Int. J. Syst. Evol. Microbiol. 66:3281-3286(2016).
RN [2] {ECO:0000313|Proteomes:UP000077317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA 26 {ECO:0000313|Proteomes:UP000077317};
RA Bai X.;
RT "Streptococcus antelopensis sp. nov., isolated from the feces of the
RT Tibetan antelope (Pantholops hodgsonii) in Hoh Xil National Nature Reserve,
RT Qinghai, China.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates the cytosine at position 967 (m5C967)
CC of 16S rRNA. {ECO:0000256|ARBA:ARBA00002724}.
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR EMBL; CP014699; AND80467.1; -; Genomic_DNA.
DR RefSeq; WP_067065225.1; NZ_CP014699.1.
DR AlphaFoldDB; A0A172QAM2; -.
DR STRING; 1811193.A0O21_07215; -.
DR KEGG; spat:A0O21_07215; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000077317; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.940.10; NusB-like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000077317};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01023};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01023};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01023}.
FT DOMAIN 162..439
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 380
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 257..263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 280
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 308
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 327
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 440 AA; 49885 MW; 31E7C05CA3400BEF CRC64;
MKNSWQKSAR GAALLILEKI FKEQAYSNIV LNRYLKQSSL TSQDKSLVTE LVYGTVARKI
TLEWYLSHFI QDRTKLEEWL YYLLLLSLYQ LLYLDNIPNH AVVNEAVALA KKRSRQRGAE
KLVNAVLRRV TEGNLPDISS IKRKNKYYSV KYSLPVWLVR KLIEQYGEKR GLDIMASLLV
RSKASIRLVN PQKKSEIMAA TGALSSQISP VGLVKSSGHF AETAYFSHGD ITIQDESSQL
VAPIMNIQGD ETILDACSAP GGKAAHMASY LTSGHIEALD LYDHKLKLII DNAKRLHVSD
RISVRKLDAR KVHDYFGKDS FDKILVDAPC SGIGLIRRKP DIKYNKELQN LAALQKIQLQ
ILESVCQTIR KGGIITYSTC TIFAEENFQV IKTFLEKHSD FEQVPLNHKQ KDIVKDGCII
ITPEQYHTDG FFISQVKRIL
//
