UniProt Accession

 RS1_ECOLI; P0AG67; P02349; P77352 

Genbank Protein ID

 V00342; V00352; U00096; AP009048; X00785; X04864 

Genbank Nucleotide ID

 CAA23630.1; CAA23644.1; AAC73997.1; BAA35655.1; CAA25361.1; CAA28556.1 

Protein Name

 30S ribosomal protein S1 

Protein Synonyms/Alias

  

Gene Name

 rpsA 

Gene Synonyms/Alias

 ssyF; b0911; JW0894 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
43	VLVDAGLKSESAIPA	acetylation	[1]
100	EAWITLEKAYEDAET	acetylation	[1]
115	VTGVINGKVKGGFTV	acetylation	[1]
150	DTLHLEGKELEFKVI	acetylation	[1, 2]
155	EGKELEFKVIKLDQK	acetylation	[1]
158	ELEFKVIKLDQKRNN	acetylation	[1]
162	KVIKLDQKRNNVVVS	acetylation	[1]
196	LQEGMEVKGIVKNLT	acetylation	[1]
229	DMAWKRVKHPSEIVN	acetylation	[1, 2, 3]
244	VGDEITVKVLKFDRE	acetylation	[1]
247	EITVKVLKFDRERTR	acetylation	[1, 4]
260	TRVSLGLKQLGEDPW	acetylation	[1]
272	DPWVAIAKRYPEGTK	acetylation	[1, 2]
279	KRYPEGTKLTGRVTN	acetylation	[1, 2, 3]
320	NKNIHPSKVVNVGDV	acetylation	[2]
350	SLGLKQCKANPWQQF	acetylation	[2]
363	QFAETHNKGDRVEGK	acetylation	[1, 3]
370	KGDRVEGKIKSITDF	acetylation	[1]
434	ERISLGVKQLAEDPF	acetylation	[1]
449	NNWVALNKKGAIVTG	acetylation	[1]
450	NWVALNKKGAIVTGK	acetylation	[1]
464	KVTAVDAKGATVELA	acetylation	[1, 2]
522	ISLSVRAKDEADEKD	acetylation	[1]
528	AKDEADEKDAIATVN	acetylation	[1]
536	DAIATVNKQEDANFS	acetylation	[1]
552	NAMAEAFKAAKGE**	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [3] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [4] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508] 

Functional Description

 Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence. 

Sequence Annotation

 DOMAIN 21 87 S1 motif 1.
 DOMAIN 105 171 S1 motif 2.
 DOMAIN 192 260 S1 motif 3.
 DOMAIN 277 347 S1 motif 4.
 DOMAIN 364 434 S1 motif 5.
 DOMAIN 451 520 S1 motif 6.
 MOD_RES 229 229 N6-acetyllysine.
 MOD_RES 279 279 N6-acetyllysine.
 MOD_RES 363 363 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein; RNA-binding. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 557 AA 

Protein Sequence

Gene Ontology

 GO:0022627; C:cytosolic small ribosomal subunit; IDA:EcoCyc.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0003729; F:mRNA binding; IDA:EcoCyc.
 GO:0003735; F:structural constituent of ribosome; IDA:EcoCyc.
 GO:2000766; P:negative regulation of cytoplasmic translation; IDA:EcoCyc.
 GO:0006412; P:translation; IMP:EcoCyc. 

Interpro

 IPR012340; NA-bd_OB-fold.
 IPR003029; Rbsml_prot_S1_RNA-bd_dom.
 IPR000110; Ribosomal_S1.
 IPR022967; RNA-binding_domain_S1. 

Pfam

 PF00575; S1 

SMART

 SM00316; S1 

PROSITE

 PS50126; S1 

PRINTS

 PR00681; RIBOSOMALS1.