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Database: UniProt
Entry: A8A593
LinkDB: A8A593
Original site: A8A593 
ID   RSMB_ECOHS              Reviewed;         429 AA.
AC   A8A593;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   11-JUN-2014, entry version 51.
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=EcHS_A3482;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic
RT   analysis of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(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 class I-like SAM-binding
CC       methyltransferase superfamily. RsmB/NOP family.
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DR   EMBL; CP000802; ABV07697.1; -; Genomic_DNA.
DR   RefSeq; YP_001460080.1; NC_009800.1.
DR   ProteinModelPortal; A8A593; -.
DR   SMR; A8A593; 5-428.
DR   STRING; 331112.EcHS_A3482; -.
DR   EnsemblBacteria; ABV07697; ABV07697; EcHS_A3482.
DR   GeneID; 5591816; -.
DR   KEGG; ecx:EcHS_A3482; -.
DR   PATRIC; 18316924; VBIEscCol77814_3390.
DR   eggNOG; COG0144; -.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; GHDGFYY; -.
DR   OrthoDB; EOG6091D0; -.
DR   BioCyc; ECOL331112:GHHI-3478-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:UniProtKB-HAMAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.940.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 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   InterPro; IPR029063; SAM-dependent_MTases-like.
DR   Pfam; PF01189; Nol1_Nop2_Fmu; 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   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_0000366159.
FT   REGION      254    260       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   ACT_SITE    375    375       Nucleophile (By similarity).
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;  48348 MW;  1F516223C84D80F8 CRC64;
     MKKQRNLRSM AAQAVEQVVE QGQSLSNILP PLQQKVSDKD KALLQELCFG VLRTLSQLDW
     LINKLMARPM TGKQRTVHYL IMVGLYQLLY TRIPPHAALA ETVEGAIAIK RPQLKGLING
     VLRQFQRQQE ELLAEFNASD ARYLHPSWLL KRLQKAYPEQ WQSIVEANNQ RPPMWLRINR
     THHSRDSWLA LLDEAGMKGF PHADYPDAVR LETPAPVHAL PGFEDGWVTV QDASAQGCMT
     WLAPQNGEHI LDLCAAPGGK TTHILEVAPE AQVVAVDIDE QRLSRVYDNL KRLGMKATVK
     QGDGRYPSQW CGEQQFDRIL LDAPCSATGV IRRHPDIKWL RRDRDIPELA QLQSEILDAI
     WPHLKTGGTL VYATCSVLPE ENSLQIKAFL QRTADAELCE TGTPEQPGKQ NLPGAEEGDG
     FFYAKLIKK
//
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