Ribosomal RNA small subunit methyltransferase C - Escherichia coli (strain K12)

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P39406 (RSMC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ribosomal RNA small subunit methyltransferase C
EC=2.1.1.172

Alternative name(s):
16S rRNA m2G1207 methyltransferase
rRNA (guanine-N(2)-)-methyltransferase RsmC

Gene names

Name:	rsmC
Synonyms:	yjjT
Ordered Locus Names:	b4371, JW4333

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Specifically methylates the guanosine in position 1207 of 16S rRNA in the 30S particle. HAMAP MF_01862
Catalytic activity	S-adenosyl-L-methionine + guanosine(1207) in 16S rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanosine(1207) in 16S rRNA. HAMAP MF_01862
Cofactor	Magnesium.
Subunit structure	Monomer. Ref.5
Subcellular location	Cytoplasm Potential HAMAP MF_01862.
Sequence similarities	Belongs to the methyltransferase superfamily. RsmC family.

Ontologies

Keywords
Biological process	rRNA processing
Cellular component	Cytoplasm
Ligand	Magnesium S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	rRNA base methylation Inferred from mutant phenotype Ref.5. Source: EcoCyc
Cellular component	cytoplasm Inferred by curator Ref.4. Source: UniProtKB
Molecular function	nucleic acid binding Inferred from electronic annotation. Source: InterPro rRNA (guanine-N2-)-methyltransferase activity Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4

Chain

2 – 343

342

Ribosomal RNA small subunit methyltransferase C HAMAP MF_01862

PRO_0000097490

Experimental info

Mutagenesis

K → S: Reduces activity by 84%; when associated with S-88. Ref.5

Mutagenesis

K → S: Reduces activity by 84%; when associated with S-86. Ref.5

Mutagenesis

202

D → A: Abolishes affinity for S-adenosyl-L-methionine. Loss of activity. Ref.5

Mutagenesis

227

D → A: Strongly reduces affinity for S-adenosyl-L-methionine. Reduces activity by 87%. Ref.5

Mutagenesis

268

N → A: Reduces affinity for S-adenosyl-L-methionine. Reduces activity by 80%. Ref.5

Secondary structure

343

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P39406 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 81E190CB86E4BAC2
Show »

FASTA

343

37,625

        10         20         30         40         50         60 
MSAFTPASEV LLRHSDDFEQ SRILFAGDLQ DDLPARLDTA ASRAHTQQFH HWQVLSRQMG 

        70         80         90        100        110        120 
DNARFSLVAT ADDVADCDTL IYYWPKNKPE AQFQLMNLLS LLPVGTDIFV VGENRSGVRS 

       130        140        150        160        170        180 
AEQMLADYAP LNKVDSARRC GLYFGRLEKQ PVFDAEKFWG EYSVDGLTVK TLPGVFSRDG 

       190        200        210        220        230        240 
LDVGSQLLLS TLTPHTKGKV LDVGCGAGVL SVAFARHSPK IRLTLCDVSA PAVEASRATL 

       250        260        270        280        290        300 
AANGVEGEVF ASNVFSEVKG RFDMIISNPP FHDGMQTSLD AAQTLIRGAV RHLNSGGELR 

       310        320        330        340 
IVANAFLPYP DVLDETFGFH EVIAQTGRFK VYRAIMTRQA KKG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed: 7610040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Purification, cloning, and characterization of the 16S RNA m2G1207 methyltransferase from Escherichia coli." Tscherne J.S., Nurse K., Popienick P., Ofengand J. J. Biol. Chem. 274:924-929(1999) [PubMed: 9873033] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-20, CHARACTERIZATION.
[5]	"Functional specialization of domains tandemly duplicated within 16S rRNA methyltransferase RsmC." Sunita S., Purta E., Durawa M., Tkaczuk K.L., Swaathi J., Bujnicki J.M., Sivaraman J. Nucleic Acids Res. 35:4264-4274(2007) [PubMed: 17576679] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), MUTAGENESIS OF LYS-86; LYS-88; ASP-202; ASP-227 AND ASN-268, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U14003 Genomic DNA. Translation: AAA97267.1.
U00096 Genomic DNA. Translation: AAC77324.1.
AP009048 Genomic DNA. Translation: BAE78359.1.

PIR

S56595.

RefSeq

NP_418788.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PJD	X-ray	2.10	A	1-343	[»]

ProteinModelPortal

P39406.

SMR

P39406. Positions 3-336.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10804N.

IntAct

P39406. 14 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001068; EBESCP00000001068; EBESCG00000000884.
EBESCT00000016850; EBESCP00000016141; EBESCG00000015909.

GeneID

948892.

GenomeReviews

Gene locus JW4333 in contig AP009048_GR.
Gene locus b4371 in contig U00096_GR.

KEGG

ecj:JW4333.
eco:b4371.

PATRIC

32124352. VBIEscCol129921_4516.

Organism-specific databases

EchoBASE

EB2481.

EcoGene

EG12596. rsmC.

Phylogenomic databases

eggNOG

COG2813.

GeneTree

EBGT00050000009812.

HOGENOM

HBG296757.

OMA

TGKFKVY.

PhylomeDB

P39406.

ProtClustDB

PRK09489.

Enzyme and pathway databases

BioCyc

EcoCyc:G7950-MONOMER.
MetaCyc:G7950-MONOMER.

BRENDA

2.1.1.52. 2026.

Gene expression databases

Genevestigator

P39406.

Family and domain databases

HAMAP

MF_01862. 16SrRNA_methyltr_C.
[Tree]

InterPro

IPR002052. DNA_methylase_N6_adenine_CS.
IPR013675. Mtase_sm_N.
IPR023543. rRNA_ssu_MeTfrase_C.
IPR007848. Small_mtfrase.
[Graphical view]

K00564.

Pfam

PF05175. MTS. 1 hit.
PF08468. MTS_N. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RSMC_ECOLI

Accession

Primary (citable) accession number: P39406
Secondary accession number(s): Q2M5U7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents