Ribosomal protein S12 methylthiotransferase RimO

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P0AEI4 (RIMO_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 68. History...

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

Documents (2) |

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 protein S12 methylthiotransferase RimO
Short name=S12 MTTase
Short name=S12 methylthiotransferase
EC=2.-.-.-

Alternative name(s):
Ribosome maturation factor RimO

Gene names

Name:	rimO
Synonyms:	yliG
Ordered Locus Names:	b0835, JW0819

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	441 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the methylthiolation of the residue Asp-89 of ribosomal protein S12. Ref.4 Ref.5
Cofactor	Binds 2 4Fe-4S clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_01865.
Disruption phenotype	Mutant shows a lack of methylthiolation of protein S12 and a decrease in transcription of a subset of genes. Ref.5
Sequence similarities	Belongs to the methylthiotransferase family. RimO subfamily. Contains 1 MTTase N-terminal domain. Contains 1 TRAM domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA modification Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from direct assay PubMed 19736993. Source: EcoCyc aspartic acid methylthiotransferase activity Inferred from direct assay PubMed 19736993. Source: EcoCyc iron ion binding 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 – 441

441

Ribosomal protein S12 methylthiotransferase RimO HAMAP-Rule MF_01865

PRO_0000141738

Regions

Domain

8 – 118

111

MTTase N-terminal

Domain

376 – 441

TRAM

Sites

Metal binding

Iron-sulfur (4Fe-4S) By similarity

Metal binding

Iron-sulfur (4Fe-4S) By similarity

Metal binding

Iron-sulfur (4Fe-4S) By similarity

Metal binding

150

Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Metal binding

154

Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Metal binding

157

Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0AEI4 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: E1D4605388AFB889
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FASTA

441

49,582

        10         20         30         40         50         60 
MSKVTPQPKI GFVSLGCPKN LVDSERILTE LRTEGYDVVP SYDDADMVIV NTCGFIDSAV 

        70         80         90        100        110        120 
QESLEAIGEA LNENGKVIVT GCLGAKEDQI REVHPKVLEI TGPHSYEQVL EHVHHYVPKP 

       130        140        150        160        170        180 
KHNPFLSLVP EQGVKLTPRH YAYLKISEGC NHRCTFCIIP SMRGDLVSRP IGEVLSEAKR 

       190        200        210        220        230        240 
LVDAGVKEIL VISQDTSAYG VDVKHRTGFH NGEPVKTSMV SLCEQLSKLG IWTRLHYVYP 

       250        260        270        280        290        300 
YPHVDDVIPL MAEGKILPYL DIPLQHASPR ILKLMKRPGS VDRQLARIKQ WREICPELTL 

       310        320        330        340        350        360 
RSTFIVGFPG ETEEDFQMLL DFLKEARLDR VGCFKYSPVE GADANALPDQ VPEEVKEERW 

       370        380        390        400        410        420 
NRFMQLQQQI SAERLQEKVG REILVIIDEV DEEGAIGRSM ADAPEIDGAV YLNGETNVKP 

       430        440 
GDILRVKVEH ADEYDLWGSR V

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli." Anton B.P., Saleh L., Benner J.S., Raleigh E.A., Kasif S., Roberts R.J. Proc. Natl. Acad. Sci. U.S.A. 105:1826-1831(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A METHYLTHIOTRANSFERASE. Strain: K12 / MG1655 / ATCC 47076.
[5]	"A proteomic and transcriptomic approach reveals new insight into beta-methylthiolation of Escherichia coli ribosomal protein S12." Strader M.B., Costantino N., Elkins C.A., Chen C.Y., Patel I., Makusky A.J., Choy J.S., Court D.L., Markey S.P., Kowalak J.A. Mol. Cell. Proteomics 10:M110.005199.01-M110.005199.10(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00096 Genomic DNA. Translation: AAC73922.1. AP009048 Genomic DNA. Translation: BAA35530.1.
PIR	C64821.
RefSeq	NP_415356.1. NC_000913.2. YP_489108.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0AEI4.
SMR	P0AEI4. Positions 139-441.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48218N.
IntAct	P0AEI4. 17 interactions.
STRING	511145.b0835.
Proteomic databases
PaxDb	P0AEI4.
PRIDE	P0AEI4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73922; AAC73922; b0835. BAA35530; BAA35530; BAA35530.
GeneID	12932851. 945465.
KEGG	ecj:Y75_p0808. eco:b0835.
PATRIC	32116873. VBIEscCol129921_0862.
Organism-specific databases
EchoBASE	EB3251.
EcoGene	EG13478. rimO.
Phylogenomic databases
eggNOG	COG0621.
HOGENOM	HOG000224766.
KO	K14441.
OMA	CPDITLR.
ProtClustDB	PRK14862.
Enzyme and pathway databases
BioCyc	EcoCyc:G6435-MONOMER. ECOL316407:JW0819-MONOMER. MetaCyc:G6435-MONOMER.
Gene expression databases
Genevestigator	P0AEI4.
Family and domain databases
Gene3D	2.40.50.140. 1 hit. 3.80.30.20. 1 hit.
HAMAP	MF_01865. MTTase_RimO.
InterPro	IPR006638. Elp3/MiaB/NifB. IPR023970. MeThioTfrase/rSAM. IPR005839. Methylthiotransferase. IPR020612. Methylthiotransferase_CS. IPR013848. Methylthiotransferase_N. IPR012340. NA-bd_OB-fold. IPR005840. Ribosomal_S12_MeSTrfase_RimO. IPR007197. rSAM. IPR023404. rSAM_horseshoe. IPR002792. TRAM_dom. [Graphical view]
PANTHER	PTHR11918. PTHR11918. 1 hit.
Pfam	PF04055. Radical_SAM. 1 hit. PF00919. UPF0004. 1 hit. [Graphical view]
SMART	SM00729. Elp3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00089. TIGR00089. 1 hit. TIGR01125. TIGR01125. 1 hit.
PROSITE	PS51449. MTTASE_N. 1 hit. PS01278. MTTASE_RADICAL. 1 hit. PS50926. TRAM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIMO_ECOLI

Accession

Primary (citable) accession number: P0AEI4
Secondary accession number(s): P75802

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 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

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

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic 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