ID RSMB_ECOSE Reviewed; 429 AA.
AC B6I202;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 01-MAY-2013, entry version 36.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase B;
DE EC=2.1.1.176;
DE AltName: Full=16S rRNA m5C967 methyltransferase;
DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB;
GN Name=rsmB; Synonyms=sun; OrderedLocusNames=ECSE_3563;
OS Escherichia coli (strain SE11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=409438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SE11;
RX PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H.,
RA Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT "Complete genome sequence and comparative analysis of the wild-type
RT commensal Escherichia coli strain SE11 isolated from a healthy
RT adult.";
RL DNA Res. 15:375-386(2008).
CC -!- FUNCTION: Specifically methylates the cytosine at position 967
CC (m5C967) of 16S rRNA (By similarity).
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytosine(967) in 16S
CC rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine(967) in 16S
CC rRNA.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmB/NOP
CC family.
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DR EMBL; AP009240; BAG79087.1; -; Genomic_DNA.
DR RefSeq; YP_002294838.1; NC_011415.1.
DR ProteinModelPortal; B6I202; -.
DR SMR; B6I202; 5-428.
DR STRING; 409438.ECSE_3563; -.
DR EnsemblBacteria; BAG79087; BAG79087; ECSE_3563.
DR GeneID; 7001948; -.
DR KEGG; ecy:ECSE_3563; -.
DR PATRIC; 18425756; VBIEscCol83070_3731.
DR eggNOG; COG0144; -.
DR HOGENOM; HOG000037300; -.
DR KO; K03500; -.
DR OMA; KPPMWLR; -.
DR ProtClustDB; PRK10901; -.
DR BioCyc; ECOL409438:GHUU-3750-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016434; F:rRNA (cytosine) methyltransferase activity; IEA:HAMAP.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR Gene3D; 1.10.940.10; -; 1.
DR HAMAP; MF_01856; 16SrRNA_methyltr_B; 1; -.
DR InterPro; IPR001678; Fmu/NOL1/Nop2p.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR006027; NusB_RsmB_TIM44.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR004573; rRNA_ssu_MeTfrase_B.
DR InterPro; IPR023541; rRNA_ssu_MeTfrase_B_ent.
DR Pfam; PF01189; Nol1_Nop2_Fmu; 1.
DR Pfam; PF01029; NusB; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF48013; NusB_RsmB_TIM44; 1.
DR TIGRFAMs; TIGR00563; rsmB; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Methyltransferase; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1 429 Ribosomal RNA small subunit
FT methyltransferase B.
FT /FTId=PRO_1000188695.
FT REGION 254 260 S-adenosyl-L-methionine binding (By
FT similarity).
FT ACT_SITE 375 375 Nucleophile (Potential).
FT BINDING 277 277 S-adenosyl-L-methionine (By similarity).
FT BINDING 303 303 S-adenosyl-L-methionine (By similarity).
FT BINDING 322 322 S-adenosyl-L-methionine (By similarity).
SQ SEQUENCE 429 AA; 48319 MW; D84166307B4D80F2 CRC64;
MKKQRNLRSM AAQAVEQVVE QGQSLSNILP PLQQKVSDKD KALLQELCFG VLRTLSQLDW
LINKLMARPM TGKQRTVHYL IMVGLYQLLY TRIPPHAALA ETVEGAIAIK RPQLKGLING
VLRQFQRQQE ELLAEFNASD ARYLHPSWLL KRLQKAYPEQ WQSIVEANNQ RPPMWLRVNR
THHSRDSWLA LLDEAGMKGF PHADYPDAVR LETPAPVHAL PGFEDGWVTV QDASAQGCMT
WLAPQNGEHI LDLCAAPGGK TTHILEVAPE AQVVAVDIDE QRLSRVYDNL KRLGMKATVK
QGDGRYPSQW CGEQQFDRIL LDAPCSATGV IRRHPDIKWL RRDRDIPELA QLQSEILDAI
WPHLKSGGTL VYATCSVLPE ENSLQIKAFL QRTADAELCE TGTPEQPGKQ NLPGAEEGDG
FFYAKLIKK
//
