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Database: UniProt
Entry: L5L9R9_9MOLU
LinkDB: L5L9R9_9MOLU
Original site: L5L9R9_9MOLU 
ID   L5L9R9_9MOLU            Unreviewed;       419 AA.
AC   L5L9R9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
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   Name=sun {ECO:0000313|EMBL:ELK20031.1};
GN   ORFNames=D500_0563 {ECO:0000313|EMBL:ELK20031.1};
OS   Mycoplasma feriruminatoris.
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=1179777 {ECO:0000313|EMBL:ELK20031.1, ECO:0000313|Proteomes:UP000010753};
RN   [1] {ECO:0000313|EMBL:ELK20031.1, ECO:0000313|Proteomes:UP000010753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G5847 {ECO:0000313|EMBL:ELK20031.1,
RC   ECO:0000313|Proteomes:UP000010753};
RX   PubMed=23469346;
RA   Fischer A., Santana-Cruz I., Giglio M., Nadendla S., Drabek E., Vilei E.M.,
RA   Frey J., Jores J.;
RT   "Genome Sequence of Mycoplasma feriruminatoris sp. nov., a Fast-Growing
RT   Mycoplasma Species.";
RL   Genome Announc. 1:E00216-12(2013).
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|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELK20031.1}.
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DR   EMBL; ANFU01000034; ELK20031.1; -; Genomic_DNA.
DR   RefSeq; WP_008363720.1; NZ_KB199604.1.
DR   AlphaFoldDB; L5L9R9; -.
DR   STRING; 1179777.D500_0563; -.
DR   PATRIC; fig|1179777.3.peg.520; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG0781; Bacteria.
DR   HOGENOM; CLU_005316_0_1_14; -.
DR   Proteomes; UP000010753; Unassembled WGS sequence.
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; 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   NCBIfam; TIGR00563; rsmB; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF53; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE B-RELATED; 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; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
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          153..419
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        371
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         251..257
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         275
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         302
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         318
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   419 AA;  48659 MW;  003AAB57965E13A6 CRC64;
     MNSRSLAFDI LKKVFINKAY SNVLLNKVSK LDIDQLEKDF VFNLVHGIIS NKIHLDYLLT
     RLIDLKKTKK ELQIILLIGL YQMIYLDNIP NYAIVNETVN LAKTINQKSA NFINAILNKF
     LRFKNKYLEI NLDNKDLELC IIHSFSYELY LMLIKQYDKQ IVNKIVINNH QIPKLYIRVN
     TLKITTDQLF NQYKDIYLLE KTNTNNCLVA NKTIINSDLY KNGLITIQDK ASILVSQILN
     PSLNTKVLDM CSAPGGKLTH LSMIMNNTGS IIGNELSESK IRLIKENILR LNCLNISLTN
     MDARDIKQKQ EFDYILLDAP CSGFGVFKRK PEIKLRFDQK QVKSIIQLQS ELLESAYYNL
     KTNGEMVYST CTINQNENQN QINKFLNKHK NMVKVFEQQI FGFEENTDGF YICKLKKQH
//
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