Reviewed, UniProtKB/Swiss-Prot P25813 (RSMG_BACSU)

Names and origin

Protein names

Recommended name:
    Ribosomal RNA small subunit methyltransferase G
    EC=2.1.1.-
Alternative name(s):
    16S rRNA 7-methylguanosine methyltransferase
      Short name=16S rRNA m7G methyltransferase
    Glucose-inhibited division protein B

Gene names

Name:	rsmG
Synonyms:	gidB
Ordered Locus Names:	BSU41000

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	239 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Specifically methylates the N7 position of guanosine in position 535 of 16S rRNA. Ref.4
Subcellular location	Cytoplasm Potential HAMAP MF_00074.
Disruption phenotype	Low-level streptomycin resistance. Ref.4
Sequence similarities	Belongs to the methyltransferase superfamily. RNA methyltransferase rsmG family.

Ontologies

Keywords
Biological process	rRNA processing
Cellular component	Cytoplasm
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	rRNA processing Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	rRNA (guanine-N7-)-methyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 239

239

Ribosomal RNA small subunit methyltransferase G HAMAP MF_00074

PRO_0000184215

Secondary structure

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239

Helix Strand Turn

Details...

Helix

3 – 12

10

Helix

19 – 38

20

Helix

47 – 53

7

Helix

55 – 59

5

Helix

60 – 63

4

Helix

67 – 69

3

Beta strand

72 – 76

5

Beta strand

78 – 80

3

Helix

84 – 90

7

Beta strand

95 – 101

7

Helix

103 – 116

14

Beta strand

119 – 126

8

Helix

128 – 131

4

Turn

135 – 139

5

Beta strand

141 – 147

7

Helix

152 – 159

8

Helix

160 – 162

3

Beta strand

163 – 173

11

Helix

178 – 190

13

Beta strand

193 – 202

10

Turn

204 – 206

3

Beta strand

209 – 217

9

Helix

231 – 234

4

Sequences

	Sequence		Length	Mass (Da)
	P25813-1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 525826A929B32AA9	FASTA	239	26,954
	10 20 30 40 50 60 MNIEEFTSGL AEKGISLSPR QLEQFELYYD MLVEWNEKIN LTSITEKKEV YLKHFYDSIT 70 80 90 100 110 120 AAFYVDFNQV NTICDVGAGA GFPSLPIKIC FPHLHVTIVD SLNKRITFLE KLSEALQLEN 130 140 150 160 170 180 TTFCHDRAET FGQRKDVRES YDIVTARAVA RLSVLSELCL PLVKKNGLFV ALKAASAEEE 190 200 210 220 230 LNAGKKAITT LGGELENIHS FKLPIEESDR NIMVIRKIKN TPKKYPRKPG TPNKSPIEG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genes and their organization in the replication origin region of the bacterial chromosome." Ogasawara N., Yoshikawa H. Mol. Microbiol. 6:629-634(1992) [PubMed: 1552862] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / CRK2000.
[2]	"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin." Ogasawara N., Nakai S., Yoshikawa H. DNA Res. 1:1-14(1994) [PubMed: 7584024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Identification of the RsmG methyltransferase target as 16S rRNA nucleotide G527 and characterization of Bacillus subtilis rsmG mutants." Nishimura K., Johansen S.K., Inaoka T., Hosaka T., Tokuyama S., Tahara Y., Okamoto S., Kawamura F., Douthwaite S., Ochi K. J. Bacteriol. 189:6068-6073(2007) [PubMed: 17573471] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE. Strain: 168.
[5]	"The 1.6 A crystal structure of Gram-positive Bacillus subtilis glucose inhibited division protein b (gidB)." Midwest center for structural genomics (MCSG) Submitted (JAN-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X62539 Genomic DNA. Translation: CAA44405.1.
D26185 Genomic DNA. Translation: BAA05230.1.
AL009126 Genomic DNA. Translation: CAB16137.1.

PIR

BWBSGB. I40441.

RefSeq

NP_391980.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XDZ	X-ray	1.60	A	1-239	[»]

ModBase

Search...

Genome annotation databases

GeneID

937931.

GenomeReviews

Gene locus BSU41000 in contig AL009126_GR.

KEGG

bsu:BSU41000.

NMPDR

fig|224308.1.peg.4106.

Organism-specific databases

SubtiList

BG10058. rsmG. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

HBG686577.

OMA

EYTLPFV.

PhylomeDB

P25813.

Family and domain databases

HAMAP

MF_00074. 16SrRNA_methyltr_G.
[Tree]

InterPro

IPR003682. rRNA_ssu_MeTfrase_G.
[Graphical view]

Pfam

PF02527. GidB. 1 hit.
[Graphical view]

PIRSF

PIRSF003078. GidB. 1 hit.

TIGRFAMs

TIGR00138. gidB. 1 hit.

ProtoNet

Search...

Entry information

Entry name

RSMG_BACSU

Accession

Primary (citable) accession number: P25813

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	February 9, 2010
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)