rpsI

rpsI
168

ribosomal protein uS9

Locus
BSU_01500
Molecular weight
14.00 kDa
Isoelectric point
11
Protein length
130 aaSequenceBlast
Gene length
393 bpSequenceBlast
Function
translation
Product
ribosomal protein S9 (uS9)
Essential
yes
Synonyms
rpsI
Outlinks
BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG0103 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
154,300 → 154,692
Phenotypes of a mutant
essential PubMed
The protein
Protein family
universal ribosomal protein uS9 family (single member, according to UniProt)
Structure
3J9W (PDB) (the ribosome) PubMed
P21470 (AlphaFold)
Modification
phosphorylated on Arg-20 PubMed
acetylated at the N-terminus PubMed
Expression and Regulation
Operons
Genes
rplM-rpsI
Description
PubMed
Regulation
Rel dependent downregulation (Class I) during stringent response PubMed
likely autorepression of rplM-rpsI expression upon binding of excess RplM to the untranslated region of the rplM-rpsI mRNA PubMed
Regulatory mechanism
stringent response: negative regulation, PubMed, in stringent response
Open in new tab

rplM->rpsI

2025-03-17 17:42:54

Jstuelk

94

1e953db547b59dcb7f45eec2da4084ab9a6fe4e8

7A67E30BD15613891F4B98B693A6AEB3A9872BEF

Genes
truA-rplM-rpsI
Description
PubMed
Regulation
Rel dependent downregulation (Class I) during stringent response PubMed
expression is reduced in motile cells as compared to non-motile cells PubMed
Regulatory mechanism
stringent response: negative regulation, PubMed, in stringent response
Open in new tab

truA->rpsI

2025-03-26 05:46:23

Jstuelk

105

9378802F22213CCB249C12ED6C7E38294E94AEBA

BCBF9D5540A2F40C69EB9BD2FDE789D8B342DBAE

References
O'Reilly FJ, Graziadei A, Forbrig C, Bremenkamp R, Charles K, Lenz S, Elfmann C, Fischer L, Stülke J, Rappsilber JProtein complexes in cells by AI-assisted structural proteomics.Molecular systems biology. 2023 Feb 23; :e11544. PMID: 36815589
Sohmen D, Chiba S, Shimokawa-Chiba N, Innis CA, Berninghausen O, Beckmann R, Ito K, Wilson DN Structure of the Bacillus subtilis 70S ribosome reveals the basis for species-specific stalling. Nature communications. 2015 Apr 23; 6:6941. doi:10.1038/ncomms7941. PMID:25903689
Akanuma G, Nanamiya H, Natori Y, Yano K, Suzuki S, Omata S, Ishizuka M, Sekine Y, Kawamura F Inactivation of ribosomal protein genes in Bacillus subtilis reveals importance of each ribosomal protein for cell proliferation and cell differentiation. Journal of bacteriology. 2012 Nov; 194(22):6282-91. doi:10.1128/JB.01544-12. PMID:23002217
Elsholz AK, Turgay K, Michalik S, Hessling B, Gronau K, Oertel D, Mäder U, Bernhardt J, Becher D, Hecker M, Gerth U Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis. Proceedings of the National Academy of Sciences of the United States of America. 2012 May 08; 109(19):7451-6. doi:10.1073/pnas.1117483109. PMID:22517742
Lauber MA, Running WE, Reilly JP B. subtilis ribosomal proteins: structural homology and post-translational modifications. Journal of proteome research. 2009 Sep; 8(9):4193-206. doi:10.1021/pr801114k. PMID:19653700
Yao Z, Barrick J, Weinberg Z, Neph S, Breaker R, Tompa M, Ruzzo WL A computational pipeline for high- throughput discovery of cis-regulatory noncoding RNA in prokaryotes. PLoS computational biology. 2007 Jul; 3(7):e126. . PMID:17616982

C8E45EDBCD0CFF353D1D66E6D77FD81E976BC0BC

Page visits: 4750

Time of last update: 2025-04-06 09:43:42

Author of last update: Jstuelk