RSMB_COXBU
ID RSMB_COXBU Reviewed; 430 AA.
AC P45679;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable ribosomal RNA small subunit methyltransferase B {ECO:0000305};
DE EC=2.1.1.176 {ECO:0000250|UniProtKB:P36929};
DE AltName: Full=16S rRNA m5C967 methyltransferase {ECO:0000250|UniProtKB:P36929};
DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB {ECO:0000250|UniProtKB:P36929};
GN Name=rsmB {ECO:0000250|UniProtKB:P36929}; Synonyms=rrmB, sun;
GN OrderedLocusNames=CBU_1915;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nine Mile phase I / Bratislava;
RX PubMed=8071197; DOI=10.1128/jb.176.17.5233-5243.1994;
RA Suhan M., Chen S.Y., Thompson H.A., Hoover T.A., Hill A., Williams J.C.;
RT "Cloning and characterization of an autonomous replication sequence from
RT Coxiella burnetii.";
RL J. Bacteriol. 176:5233-5243(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
CC -!- FUNCTION: Specifically methylates the cytosine at position 967 (m5C967)
CC of 16S rRNA. {ECO:0000250|UniProtKB:P36929}.
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:0000250|UniProtKB:P36929};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P36929}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA56914.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U10529; AAA56914.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE016828; AAO91406.1; -; Genomic_DNA.
DR PIR; I40649; I40649.
DR RefSeq; NP_820892.1; NC_002971.3.
DR RefSeq; WP_010958533.1; NC_002971.4.
DR AlphaFoldDB; P45679; -.
DR SMR; P45679; -.
DR STRING; 227377.CBU_1915; -.
DR DNASU; 1209828; -.
DR EnsemblBacteria; AAO91406; AAO91406; CBU_1915.
DR GeneID; 1209828; -.
DR KEGG; cbu:CBU_1915; -.
DR PATRIC; fig|227377.7.peg.1899; -.
DR eggNOG; COG0144; Bacteria.
DR HOGENOM; CLU_005316_0_4_6; -.
DR OMA; RVNRQHH; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR Gene3D; 1.10.940.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR031341; Methyltr_RsmF_N.
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 PANTHER; PTHR22807; PTHR22807; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF17125; Methyltr_RsmF_N; 1.
DR Pfam; PF01029; NusB; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF48013; SSF48013; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00563; rsmB; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..430
FT /note="Probable ribosomal RNA small subunit
FT methyltransferase B"
FT /id="PRO_0000211816"
FT ACT_SITE 371
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 246..252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 270
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 299
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 318
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 430 AA; 48950 MW; B2642AD03DA4C9B6 CRC64;
MNTRATTAIL VNQVVQKKCS LTALLSANKK NQSLIQELCY GTLRWYFKLK LIAEKLLHAP
LRDKDHDIFC LILTGFYQLN YLNIPTHTIV NQTVGAAEIL KKPWAKGLIN KLLRRFIAEK
DELLTFTEKT IEGQYAHPLW FIQHIKKAWP DHWESILIAN NARPPMTLRV NLTKISREIY
LEMLDQKNIS AKPLDFLPAA IQLEKPCSVH QLPGFNEGYC YIQDAAGQFA AYLLKLENNQ
TVLDACAAPG SKTSHILEVN PHLKTLVAID NNKQRLNRIK ENITRLGLRQ EHLQCLLADV
SQIDQWSSGE LFDRILLDAP CSATGVIRRH PDIKLLRQPG DISQYHQKKL QLLNALWTVL
KAGGFLLYST CSVLPDENEK VIEEFLSTHD KVELSPTNVH GGLQLKYGVQ QLPGQDNKDG
FYYSLLFKNP
