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Database: UniProt
Entry: A0A0R2K2E5_9LACO
LinkDB: A0A0R2K2E5_9LACO
Original site: A0A0R2K2E5_9LACO 
ID   A0A0R2K2E5_9LACO        Unreviewed;       448 AA.
AC   A0A0R2K2E5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=IV43_GL001364 {ECO:0000313|EMBL:KRN83736.1}, LAC1533_1024
GN   {ECO:0000313|EMBL:SFV40444.1};
OS   Ligilactobacillus acidipiscis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=89059 {ECO:0000313|EMBL:KRN83736.1, ECO:0000313|Proteomes:UP000051491};
RN   [1] {ECO:0000313|EMBL:KRN83736.1, ECO:0000313|Proteomes:UP000051491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15353 {ECO:0000313|EMBL:KRN83736.1,
RC   ECO:0000313|Proteomes:UP000051491};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
RN   [2] {ECO:0000313|EMBL:SFV40444.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACA-DC 1533 {ECO:0000313|EMBL:SFV40444.1};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000190935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACA-DC 1533 {ECO:0000313|Proteomes:UP000190935};
RA   Papadimitriou K.;
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; JQBK01000039; KRN83736.1; -; Genomic_DNA.
DR   EMBL; LT630287; SFV40444.1; -; Genomic_DNA.
DR   RefSeq; WP_010496244.1; NZ_LT630287.1.
DR   AlphaFoldDB; A0A0R2K2E5; -.
DR   STRING; 89059.LAC1533_1024; -.
DR   KEGG; laca:LAC1533_1024; -.
DR   PATRIC; fig|89059.3.peg.1466; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000051491; Unassembled WGS sequence.
DR   Proteomes; UP000190935; Chromosome i.
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};
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          173..447
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        386
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         262..268
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         286
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         314
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         333
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   448 AA;  50149 MW;  7EED86C16A3FF54B CRC64;
     MTSKIKNSPR YLAVNDLTRI EKENSYSNKV VDQTVAAGKL VGRDINLYTN LVYGTIQNKL
     TLDFFLKPFL KKPKKLDLWV KELLRISVYQ LGYLDRIPEH AIFNEAIEIA KQMGHEGTRR
     FVTGVLHAVS RQGLPKISEI KDPVEKLSVQ TSTPRWLVDR LLIELDPKKV SSLLQSTLKT
     PAQSVRVNNK ISDPKEVQQI LKSEGFDVSP SRVSPAVLLV QGGFIPQSRA YKAGQVTVQD
     ESASLSVESM NIQPDDQVLD MCAAPGGKTT QIAEHLNDNG HVEALDIHKN KLRLIQRNVD
     RMHLSESVTT RALDARKSPE KYSRETFDKV LVDAPCSGLG LLRRKPEIKY EKSLADTTKL
     AQVQLSILQA AAPLVAKGGQ LTYSTCTIIS TENQAVVDKF LTANPDFVQV KTTTKYHLKD
     ERQSLSLTIY PDDYDSDGFF IATLFKQK
//
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