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B6I202 (RSMB_ECOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribosomal RNA small subunit methyltransferase B
EC=2.1.1.176
Alternative name(s):
16S rRNA m5C967 methyltransferase
rRNA (cytosine-C(5)-)-methyltransferase RsmB
Gene names
Name:rsmB
Synonyms:sun
Ordered Locus Names:ECSE_3563
OrganismEscherichia coli (strain SE11) [Complete proteome] [HAMAP]
Taxonomic identifier409438 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA By similarity. HAMAP-Rule MF_01856

Catalytic activity

S-adenosyl-L-methionine + cytosine(967) in 16S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine(967) in 16S rRNA. HAMAP-Rule MF_01856

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_01856.

Sequence similarities

Belongs to the methyltransferase superfamily. RsmB/NOP family.

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentCytoplasm
   LigandRNA-binding
S-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processregulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

rRNA (cytosine) methyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 429429Ribosomal RNA small subunit methyltransferase B HAMAP-Rule MF_01856
PRO_1000188695

Regions

Region254 – 2607S-adenosyl-L-methionine binding By similarity

Sites

Active site3751Nucleophile Potential
Binding site2771S-adenosyl-L-methionine By similarity
Binding site3031S-adenosyl-L-methionine By similarity
Binding site3221S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
B6I202 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: D84166307B4D80F2

FASTA42948,319
        10         20         30         40         50         60 
MKKQRNLRSM AAQAVEQVVE QGQSLSNILP PLQQKVSDKD KALLQELCFG VLRTLSQLDW 

        70         80         90        100        110        120 
LINKLMARPM TGKQRTVHYL IMVGLYQLLY TRIPPHAALA ETVEGAIAIK RPQLKGLING 

       130        140        150        160        170        180 
VLRQFQRQQE ELLAEFNASD ARYLHPSWLL KRLQKAYPEQ WQSIVEANNQ RPPMWLRVNR 

       190        200        210        220        230        240 
THHSRDSWLA LLDEAGMKGF PHADYPDAVR LETPAPVHAL PGFEDGWVTV QDASAQGCMT 

       250        260        270        280        290        300 
WLAPQNGEHI LDLCAAPGGK TTHILEVAPE AQVVAVDIDE QRLSRVYDNL KRLGMKATVK 

       310        320        330        340        350        360 
QGDGRYPSQW CGEQQFDRIL LDAPCSATGV IRRHPDIKWL RRDRDIPELA QLQSEILDAI 

       370        380        390        400        410        420 
WPHLKSGGTL VYATCSVLPE ENSLQIKAFL QRTADAELCE TGTPEQPGKQ NLPGAEEGDG 


FFYAKLIKK

« Hide

References

[1]"Complete genome sequence and comparative analysis of the wild-type commensal Escherichia coli strain SE11 isolated from a healthy adult."
Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.
DNA Res. 15:375-386(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SE11.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009240 Genomic DNA. Translation: BAG79087.1.
RefSeqYP_002294838.1. NC_011415.1.

3D structure databases

ProteinModelPortalB6I202.
SMRB6I202. Positions 5-428.
ModBaseSearch...

Protein-protein interaction databases

STRING409438.ECSE_3563.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG79087; BAG79087; ECSE_3563.
GeneID7001948.
KEGGecy:ECSE_3563.
PATRIC18425756. VBIEscCol83070_3731.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0144.
HOGENOMHOG000037300.
KOK03500.
OMAKPPMWLR.
ProtClustDBPRK10901.

Enzyme and pathway databases

BioCycECOL409438:GHUU-3750-MONOMER.

Family and domain databases

Gene3D1.10.940.10. 1 hit.
HAMAPMF_01856. 16SrRNA_methyltr_B.
InterProIPR001678. Fmu/NOL1/Nop2p.
IPR018314. Fmu/NOL1/Nop2p_CS.
IPR006027. NusB_RsmB_TIM44.
IPR023267. RCMT.
IPR004573. rRNA_ssu_MeTfrase_B.
IPR023541. rRNA_ssu_MeTfrase_B_ent.
[Graphical view]
PfamPF01189. Nol1_Nop2_Fmu. 1 hit.
PF01029. NusB. 1 hit.
[Graphical view]
PRINTSPR02008. RCMTFAMILY.
SUPFAMSSF48013. NusB_RsmB_TIM44. 1 hit.
TIGRFAMsTIGR00563. rsmB. 1 hit.
PROSITEPS01153. NOL1_NOP2_SUN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRSMB_ECOSE
AccessionPrimary (citable) accession number: B6I202
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: December 16, 2008
Last modified: May 1, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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