UniProtKB - P0A7S9 (RS13_ECOLI)
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Protein
30S ribosomal protein S13
Gene
rpsM
Organism
Escherichia coli (strain K12)
Status
Functioni
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA.1 Publication
In the E.coli 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; bridge B1a is broken in the model with bound EF-G, while the protein-protein contacts between S13 and L5 in B1b change (PubMed:12809609). The 23S rRNA contact site in bridge B1a is modeled to differ in different ribosomal states (PubMed:16272117), contacting alternately S13 or S19. In the two 3.5 angstroms resolved ribosome structures (PubMed:12859903) the contacts between L5, S13 and S19 bridge B1b are different, confirming the dynamic nature of this interaction. Bridge B1a is not visible in the crystallized ribosomes due to 23S rRNA disorder.4 Publications
Contacts the tRNAs in the A and P sites.1 Publication
The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs.1 Publication
GO - Molecular functioni
- rRNA binding Source: UniProtKB-KW
- structural constituent of ribosome Source: GO_Central
- tRNA binding Source: UniProtKB-KW
GO - Biological processi
- ribosome biogenesis Source: GO_Central
- translation Source: GO_Central
Keywordsi
Molecular function | Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding, tRNA-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10912-MONOMER MetaCyc:EG10912-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: 30S ribosomal protein S13Alternative name(s): Small ribosomal subunit protein uS131 Publication |
Gene namesi | Name:rpsM Ordered Locus Names:b3298, JW3260 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Organism-specific databases
EcoGenei | EG10912 rpsM |
Subcellular locationi
GO - Cellular componenti
- cytosol Source: EcoCyc
- cytosolic small ribosomal subunit Source: EcoliWiki
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 83 – 118 | Missing : Decreased growth rate at all temperatures. Decreased affinity of the 30S subunit P site for tRNA in vitro. 1 PublicationAdd BLAST | 36 | |
Mutagenesisi | 114 – 118 | Missing : Decreased growth rate at all temperatures. Decreased affinity of the 30S subunit P site for tRNA in vitro. 1 Publication | 5 |
Chemistry databases
DrugBanki | DB00560 Tigecycline |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000132089 | 2 – 118 | 30S ribosomal protein S13Add BLAST | 117 |
Proteomic databases
EPDi | P0A7S9 |
PaxDbi | P0A7S9 |
PRIDEi | P0A7S9 |
Interactioni
Subunit structurei
Part of the 30S ribosomal subunit (PubMed:330375, PubMed:3279034, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:12859903, PubMed:27934701, PubMed:12244297, PubMed:27906160, PubMed:27906161). Forms a loose heterodimer with protein S19 (PubMed:3279034). Cross-links to the P site tRNA and weakly to the A site tRNA (PubMed:8524654). Forms two bridges to the 50S subunit in the 70S ribosome, contacting the 16S rRNA and proteins S19 and L5 (PubMed:12809609, PubMed:16272117, PubMed:12859903).11 Publications
Protein-protein interaction databases
DIPi | DIP-35855N |
IntActi | P0A7S9 108 interactors. |
STRINGi | 316385.ECDH10B_3473 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Beta strandi | 5 – 7 | Combined sources | 3 | |
Beta strandi | 12 – 14 | Combined sources | 3 | |
Helixi | 15 – 19 | Combined sources | 5 | |
Turni | 21 – 24 | Combined sources | 4 | |
Helixi | 28 – 36 | Combined sources | 9 | |
Beta strandi | 41 – 43 | Combined sources | 3 | |
Beta strandi | 45 – 47 | Combined sources | 3 | |
Helixi | 50 – 60 | Combined sources | 11 | |
Beta strandi | 61 – 63 | Combined sources | 3 | |
Helixi | 67 – 83 | Combined sources | 17 | |
Helixi | 86 – 92 | Combined sources | 7 | |
Turni | 97 – 99 | Combined sources | 3 | |
Beta strandi | 102 – 104 | Combined sources | 3 | |
Helixi | 107 – 109 | Combined sources | 3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1M5G | model | - | M | 2-118 | [»] | |
2YKR | electron microscopy | 9.80 | M | 2-115 | [»] | |
3J9Y | electron microscopy | 3.90 | m | 1-118 | [»] | |
3J9Z | electron microscopy | 3.60 | SM | 2-118 | [»] | |
3JA1 | electron microscopy | 3.60 | SM | 2-118 | [»] | |
3JBU | electron microscopy | 3.64 | M | 1-118 | [»] | |
3JBV | electron microscopy | 3.32 | M | 1-118 | [»] | |
3JCD | electron microscopy | 3.70 | m | 1-118 | [»] | |
3JCE | electron microscopy | 3.20 | m | 1-118 | [»] | |
3JCJ | electron microscopy | 3.70 | s | 1-118 | [»] | |
3JCN | electron microscopy | 4.60 | n | 1-118 | [»] | |
4A2I | electron microscopy | 16.50 | M | 2-115 | [»] | |
4ADV | electron microscopy | 13.50 | M | 2-118 | [»] | |
4U1U | X-ray | 2.95 | AM/CM | 2-115 | [»] | |
4U1V | X-ray | 3.00 | AM/CM | 2-115 | [»] | |
4U20 | X-ray | 2.90 | AM/CM | 2-115 | [»] | |
4U24 | X-ray | 2.90 | AM/CM | 2-115 | [»] | |
4U25 | X-ray | 2.90 | AM/CM | 2-115 | [»] | |
4U26 | X-ray | 2.80 | AM/CM | 2-115 | [»] | |
4U27 | X-ray | 2.80 | AM/CM | 2-115 | [»] | |
4V47 | electron microscopy | 12.30 | BM | 2-118 | [»] | |
4V48 | electron microscopy | 11.50 | BM | 2-118 | [»] | |
4V4H | X-ray | 3.46 | AM/CM | 1-118 | [»] | |
4V4Q | X-ray | 3.46 | AM/CM | 2-118 | [»] | |
4V4V | electron microscopy | 15.00 | AM | 2-116 | [»] | |
4V4W | electron microscopy | 15.00 | AM | 2-116 | [»] | |
4V50 | X-ray | 3.22 | AM/CM | 2-118 | [»] | |
4V52 | X-ray | 3.21 | AM/CM | 2-118 | [»] | |
4V53 | X-ray | 3.54 | AM/CM | 2-118 | [»] | |
4V54 | X-ray | 3.30 | AM/CM | 2-118 | [»] | |
4V55 | X-ray | 4.00 | AM/CM | 2-118 | [»] | |
4V56 | X-ray | 3.93 | AM/CM | 2-118 | [»] | |
4V57 | X-ray | 3.50 | AM/CM | 2-118 | [»] | |
4V5B | X-ray | 3.74 | BM/DM | 2-118 | [»] | |
4V5H | electron microscopy | 5.80 | AM | 2-114 | [»] | |
4V5Y | X-ray | 4.45 | AM/CM | 2-118 | [»] | |
4V64 | X-ray | 3.50 | AM/CM | 2-118 | [»] | |
4V65 | electron microscopy | 9.00 | AF | 1-118 | [»] | |
4V66 | electron microscopy | 9.00 | AF | 1-118 | [»] | |
4V69 | electron microscopy | 6.70 | AM | 2-114 | [»] | |
4V6C | X-ray | 3.19 | AM/CM | 1-118 | [»] | |
4V6D | X-ray | 3.81 | AM/CM | 1-118 | [»] | |
4V6E | X-ray | 3.71 | AM/CM | 1-118 | [»] | |
4V6K | electron microscopy | 8.25 | BQ | 1-118 | [»] | |
4V6L | electron microscopy | 13.20 | AQ | 1-118 | [»] | |
4V6N | electron microscopy | 12.10 | BP | 2-118 | [»] | |
4V6O | electron microscopy | 14.70 | AP | 2-118 | [»] | |
4V6P | electron microscopy | 13.50 | AP | 2-118 | [»] | |
4V6Q | electron microscopy | 11.50 | AP | 2-118 | [»] | |
4V6R | electron microscopy | 11.50 | AP | 2-118 | [»] | |
4V6S | electron microscopy | 13.10 | BO | 2-118 | [»] | |
4V6T | electron microscopy | 8.30 | AM | 2-115 | [»] | |
4V6V | electron microscopy | 9.80 | AM | 2-118 | [»] | |
4V6Y | electron microscopy | 12.00 | AM | 1-114 | [»] | |
4V6Z | electron microscopy | 12.00 | AM | 1-114 | [»] | |
4V70 | electron microscopy | 17.00 | AM | 1-114 | [»] | |
4V71 | electron microscopy | 20.00 | AM | 1-114 | [»] | |
4V72 | electron microscopy | 13.00 | AM | 1-114 | [»] | |
4V73 | electron microscopy | 15.00 | AM | 1-114 | [»] | |
4V74 | electron microscopy | 17.00 | AM | 1-114 | [»] | |
4V75 | electron microscopy | 12.00 | AM | 1-114 | [»] | |
4V76 | electron microscopy | 17.00 | AM | 1-114 | [»] | |
4V77 | electron microscopy | 17.00 | AM | 1-114 | [»] | |
4V78 | electron microscopy | 20.00 | AM | 1-114 | [»] | |
4V79 | electron microscopy | 15.00 | AM | 1-114 | [»] | |
4V7A | electron microscopy | 9.00 | AM | 1-114 | [»] | |
4V7B | electron microscopy | 6.80 | AM | 1-118 | [»] | |
4V7C | electron microscopy | 7.60 | AM | 2-118 | [»] | |
4V7D | electron microscopy | 7.60 | BM | 2-118 | [»] | |
4V7I | electron microscopy | 9.60 | BM | 1-118 | [»] | |
4V7S | X-ray | 3.25 | AM | 2-115 | [»] | |
CM | 2-114 | [»] | ||||
4V7T | X-ray | 3.19 | AM | 2-115 | [»] | |
CM | 2-114 | [»] | ||||
4V7U | X-ray | 3.10 | AM/CM | 2-115 | [»] | |
4V7V | X-ray | 3.29 | AM | 2-115 | [»] | |
CM | 2-114 | [»] | ||||
4V85 | X-ray | 3.20 | M | 1-118 | [»] | |
4V89 | X-ray | 3.70 | AM | 1-118 | [»] | |
4V9C | X-ray | 3.30 | AM/CM | 1-118 | [»] | |
4V9D | X-ray | 3.00 | AM/BM | 2-115 | [»] | |
4V9O | X-ray | 2.90 | BM/DM/FM/HM | 1-118 | [»] | |
4V9P | X-ray | 2.90 | BM/DM/FM/HM | 1-118 | [»] | |
4WF1 | X-ray | 3.09 | AM/CM | 2-115 | [»] | |
4WOI | X-ray | 3.00 | AM/DM | 1-118 | [»] | |
4WWW | X-ray | 3.10 | QM/XM | 2-115 | [»] | |
4YBB | X-ray | 2.10 | AM/BM | 2-115 | [»] | |
5AFI | electron microscopy | 2.90 | m | 1-118 | [»] | |
5H5U | electron microscopy | 3.00 | t | 2-118 | [»] | |
5IQR | electron microscopy | 3.00 | r | 1-118 | [»] | |
5IT8 | X-ray | 3.12 | AM/BM | 2-115 | [»] | |
5J5B | X-ray | 2.80 | AM/BM | 2-115 | [»] | |
5J7L | X-ray | 3.00 | AM/BM | 2-115 | [»] | |
5J88 | X-ray | 3.32 | AM/BM | 2-115 | [»] | |
5J8A | X-ray | 3.10 | AM/BM | 2-115 | [»] | |
5J91 | X-ray | 2.96 | AM/BM | 2-115 | [»] | |
5JC9 | X-ray | 3.03 | AM/BM | 2-115 | [»] | |
5JTE | electron microscopy | 3.60 | AM | 1-118 | [»] | |
5JU8 | electron microscopy | 3.60 | AM | 1-118 | [»] | |
5KCR | electron microscopy | 3.60 | 1m | 1-118 | [»] | |
5KCS | electron microscopy | 3.90 | 1m | 1-118 | [»] | |
5KPS | electron microscopy | 3.90 | 18 | 1-118 | [»] | |
5KPV | electron microscopy | 4.10 | 17 | 1-118 | [»] | |
5KPW | electron microscopy | 3.90 | 17 | 1-118 | [»] | |
5KPX | electron microscopy | 3.90 | 17 | 1-118 | [»] | |
5L3P | electron microscopy | 3.70 | m | 1-118 | [»] | |
5LZA | electron microscopy | 3.60 | m | 2-115 | [»] | |
5LZB | electron microscopy | 5.30 | m | 2-115 | [»] | |
5LZC | electron microscopy | 4.80 | m | 2-115 | [»] | |
5LZD | electron microscopy | 3.40 | m | 2-115 | [»] | |
5LZE | electron microscopy | 3.50 | m | 2-115 | [»] | |
5LZF | electron microscopy | 4.60 | m | 2-115 | [»] | |
5MDV | electron microscopy | 2.97 | r | 1-118 | [»] | |
5MDW | electron microscopy | 3.06 | r | 1-118 | [»] | |
5MDY | electron microscopy | 3.35 | r | 1-118 | [»] | |
5MDZ | electron microscopy | 3.10 | r | 1-118 | [»] | |
5ME0 | electron microscopy | 13.50 | M | 1-118 | [»] | |
5ME1 | electron microscopy | 13.50 | M | 1-118 | [»] | |
5MGP | electron microscopy | 3.10 | m | 2-115 | [»] | |
5MY1 | electron microscopy | 7.60 | M | 2-118 | [»] | |
5NO2 | electron microscopy | 5.16 | M | 2-115 | [»] | |
5NO3 | electron microscopy | 5.16 | M | 2-115 | [»] | |
5NO4 | electron microscopy | 5.16 | M | 2-115 | [»] | |
5NP6 | electron microscopy | 3.60 | P | 2-115 | [»] | |
5NWY | electron microscopy | 2.93 | C | 1-118 | [»] | |
5O2R | electron microscopy | 3.40 | m | 2-115 | [»] | |
5U4I | electron microscopy | 3.50 | m | 1-118 | [»] | |
5U9F | electron microscopy | 3.20 | M | 1-118 | [»] | |
5U9G | electron microscopy | 3.20 | M | 1-118 | [»] | |
5UYK | electron microscopy | 3.90 | M | 2-115 | [»] | |
5UYL | electron microscopy | 3.60 | M | 2-115 | [»] | |
5UYM | electron microscopy | 3.20 | M | 2-115 | [»] | |
5UYN | electron microscopy | 4.00 | M | 2-115 | [»] | |
5UYP | electron microscopy | 3.90 | M | 2-115 | [»] | |
5UYQ | electron microscopy | 3.80 | M | 2-115 | [»] | |
5UZ4 | electron microscopy | 5.80 | M | 1-118 | [»] | |
6BU8 | electron microscopy | 3.50 | M | 2-115 | [»] | |
6C4I | electron microscopy | 3.24 | m | 1-118 | [»] | |
6ENF | electron microscopy | 3.20 | m | 2-115 | [»] | |
6ENJ | electron microscopy | 3.70 | m | 2-115 | [»] | |
6ENU | electron microscopy | 3.10 | m | 2-115 | [»] | |
ProteinModelPortali | P0A7S9 | |||||
SMRi | P0A7S9 | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A7S9 |
Family & Domainsi
Sequence similaritiesi
Belongs to the universal ribosomal protein uS13 family.Curated
Phylogenomic databases
eggNOGi | ENOG4108Z04 Bacteria COG0099 LUCA |
HOGENOMi | HOG000039879 |
InParanoidi | P0A7S9 |
KOi | K02952 |
OMAi | RTKNNSR |
PhylomeDBi | P0A7S9 |
Family and domain databases
Gene3Di | 4.10.910.101 hit |
HAMAPi | MF_01315 Ribosomal_S13_S18, 1 hit |
InterProi | View protein in InterPro IPR027437 30s_Rbsml_prot_S13_C IPR001892 Ribosomal_S13 IPR010979 Ribosomal_S13-like_H2TH IPR019980 Ribosomal_S13_bac-type IPR018269 Ribosomal_S13_CS |
PANTHERi | PTHR10871:SF1 PTHR10871:SF1, 1 hit |
Pfami | View protein in Pfam PF00416 Ribosomal_S13, 1 hit |
PIRSFi | PIRSF002134 Ribosomal_S13, 1 hit |
SUPFAMi | SSF46946 SSF46946, 1 hit |
TIGRFAMsi | TIGR03631 uS13_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00646 RIBOSOMAL_S13_1, 1 hit PS50159 RIBOSOMAL_S13_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0A7S9-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MARIAGINIP DHKHAVIALT SIYGVGKTRS KAILAAAGIA EDVKISELSE
60 70 80 90 100
GQIDTLRDEV AKFVVEGDLR REISMSIKRL MDLGCYRGLR HRRGLPVRGQ
110
RTKTNARTRK GPRKPIKK
Mass spectrometryi
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 89 – 99 | Missing in PW118; partially suppresses a rimM deletion. 1 PublicationAdd BLAST | 11 | |
Natural varianti | 100 – 118 | Missing in rpsM413; pseudorevertant of streptomycin resistance. A strong antisuppressor of two tRNA suppressors, decreases translation step time and growth rate. 1 PublicationAdd BLAST | 19 | |
Natural varianti | 105 | N → H in PW095; partially suppresses a rimM deletion. 1 Publication | 1 | |
Natural varianti | 105 | N → K in PW097; partially suppresses a rimM deletion. 1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X02543 Genomic DNA Translation: CAA26392.1 U18997 Genomic DNA Translation: AAA58093.1 U00096 Genomic DNA Translation: AAC76323.1 AP009048 Genomic DNA Translation: BAE77993.1 M12432 Genomic DNA Translation: AAA83903.1 M10213 Genomic DNA Translation: AAA72457.1 |
PIRi | A23807 R3EC13 |
RefSeqi | NP_417757.1, NC_000913.3 WP_000090775.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC76323; AAC76323; b3298 BAE77993; BAE77993; BAE77993 |
GeneIDi | 947791 |
KEGGi | ecj:JW3260 eco:b3298 |
PATRICi | fig|1411691.4.peg.3433 |
Similar proteinsi
Entry informationi
Entry namei | RS13_ECOLI | |
Accessioni | P0A7S9Primary (citable) accession number: P0A7S9 Secondary accession number(s): P02369, Q2M6W3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 23, 2007 | |
Last modified: | April 25, 2018 | |
This is version 135 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |