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Database: UniProt
Entry: A0A1M6EQH5_9VIBR
LinkDB: A0A1M6EQH5_9VIBR
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ID   A0A1M6EQH5_9VIBR        Unreviewed;       428 AA.
AC   A0A1M6EQH5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=rsmB {ECO:0000313|EMBL:SHI87695.1};
GN   ORFNames=VA7868_04502 {ECO:0000313|EMBL:SHI87695.1};
OS   Vibrio aerogenes CECT 7868.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1216006 {ECO:0000313|EMBL:SHI87695.1, ECO:0000313|Proteomes:UP000184608};
RN   [1] {ECO:0000313|EMBL:SHI87695.1, ECO:0000313|Proteomes:UP000184608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7868 {ECO:0000313|EMBL:SHI87695.1,
RC   ECO:0000313|Proteomes:UP000184608};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQXZ01000051; SHI87695.1; -; Genomic_DNA.
DR   RefSeq; WP_073606087.1; NZ_FQXZ01000051.1.
DR   AlphaFoldDB; A0A1M6EQH5; -.
DR   STRING; 1216006.VA7868_04502; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000184608; 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   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   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; 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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000184608};
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          161..425
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        372
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         274
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         300
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         319
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   428 AA;  48556 MW;  A8E575888AE7AB4C CRC64;
     MNVRSAAASV IYQVVDKGVS LSTVLPEFQQ RIKTRDHALL QEICFGVLRH LPQLEGIVRQ
     LMDKPLKGKQ RVFHHLLLVG IYQIKMMRIP DHAAVGETVN ATLDLKGPKL RGLINAVLRN
     YQRRQEELES RLSESESVQY CHPGWFIRVI KESYPEHWQD IFAANNNKAP MWLRVNRSVH
     SRDEYIQLLK DSNIDVHLHS EAEDAIKLAA PCDVSSLPGF SQGWVSVQDA AAQLSVRYLN
     PKAKELILDC CAAPGGKTAH ILEHVPDARV VSVDNDESRL KRVYENLNRL NIQAEVICGD
     ARYPQKWWQG ETFDRILLDA PCSATGVIRR HPDIKWLRRL EDIDALATIQ SDILDAMWAQ
     LKPGGTMVYA TCSIMPQENS EQIKAFISRT TDVQLVDSEA ENPGRQILPG EEDMDGFYYA
     VLRKHGKK
//
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