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Protein

30S ribosomal protein S13

Gene

rpsM

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10912-MONOMER
MetaCyc:EG10912-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S13
Alternative name(s):
Small ribosomal subunit protein uS131 Publication
Gene namesi
Name:rpsM
Ordered Locus Names:b3298, JW3260
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10912 rpsM

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic small ribosomal subunit Source: EcoliWiki

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi83 – 118Missing : Decreased growth rate at all temperatures. Decreased affinity of the 30S subunit P site for tRNA in vitro. 1 PublicationAdd BLAST36
Mutagenesisi114 – 118Missing : Decreased growth rate at all temperatures. Decreased affinity of the 30S subunit P site for tRNA in vitro. 1 Publication5

Chemistry databases

DrugBankiDB00560 Tigecycline

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001320892 – 11830S ribosomal protein S13Add BLAST117

Proteomic databases

EPDiP0A7S9
PaxDbiP0A7S9
PRIDEiP0A7S9

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

DIPiDIP-35855N
IntActiP0A7S9, 108 interactors
STRINGi316385.ECDH10B_3473

Structurei

Secondary structure

1118
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0A7S9
SMRiP0A7S9
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7S9

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108Z04 Bacteria
COG0099 LUCA
HOGENOMiHOG000039879
InParanoidiP0A7S9
KOiK02952
PhylomeDBiP0A7S9

Family and domain databases

Gene3Di4.10.910.10, 1 hit
HAMAPiMF_01315 Ribosomal_S13_S18, 1 hit
InterProiView 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
PANTHERiPTHR10871:SF1 PTHR10871:SF1, 1 hit
PfamiView protein in Pfam
PF00416 Ribosomal_S13, 1 hit
PIRSFiPIRSF002134 Ribosomal_S13, 1 hit
SUPFAMiSSF46946 SSF46946, 1 hit
TIGRFAMsiTIGR03631 uS13_bact, 1 hit
PROSITEiView protein in PROSITE
PS00646 RIBOSOMAL_S13_1, 1 hit
PS50159 RIBOSOMAL_S13_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7S9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARIAGINIP DHKHAVIALT SIYGVGKTRS KAILAAAGIA EDVKISELSE
60 70 80 90 100
GQIDTLRDEV AKFVVEGDLR REISMSIKRL MDLGCYRGLR HRRGLPVRGQ
110
RTKTNARTRK GPRKPIKK
Length:118
Mass (Da):13,099
Last modified:January 23, 2007 - v2
Checksum:i6277C365EBE4F732
GO

Mass spectrometryi

Molecular mass is 12968.1 Da from positions 2 - 118. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti89 – 99Missing in PW118; partially suppresses a rimM deletion. 1 PublicationAdd BLAST11
Natural varianti100 – 118Missing in rpsM413; pseudorevertant of streptomycin resistance. A strong antisuppressor of two tRNA suppressors, decreases translation step time and growth rate. 1 PublicationAdd BLAST19
Natural varianti105N → H in PW095; partially suppresses a rimM deletion. 1 Publication1
Natural varianti105N → K in PW097; partially suppresses a rimM deletion. 1 Publication1

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
PIRiA23807 R3EC13
RefSeqiNP_417757.1, NC_000913.3
WP_000090775.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76323; AAC76323; b3298
BAE77993; BAE77993; BAE77993
GeneIDi947791
KEGGiecj:JW3260
eco:b3298
PATRICifig|1411691.4.peg.3433

Similar proteinsi

Cross-referencesi

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
PIRiA23807 R3EC13
RefSeqiNP_417757.1, NC_000913.3
WP_000090775.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-M2-118[»]
2YKRelectron microscopy9.80M2-115[»]
3J9Yelectron microscopy3.90m1-118[»]
3J9Zelectron microscopy3.60SM2-118[»]
3JA1electron microscopy3.60SM2-118[»]
3JBUelectron microscopy3.64M1-118[»]
3JBVelectron microscopy3.32M1-118[»]
3JCDelectron microscopy3.70m1-118[»]
3JCEelectron microscopy3.20m1-118[»]
3JCJelectron microscopy3.70s1-118[»]
3JCNelectron microscopy4.60n1-118[»]
4A2Ielectron microscopy16.50M2-115[»]
4ADVelectron microscopy13.50M2-118[»]
4U1UX-ray2.95AM/CM2-115[»]
4U1VX-ray3.00AM/CM2-115[»]
4U20X-ray2.90AM/CM2-115[»]
4U24X-ray2.90AM/CM2-115[»]
4U25X-ray2.90AM/CM2-115[»]
4U26X-ray2.80AM/CM2-115[»]
4U27X-ray2.80AM/CM2-115[»]
4V47electron microscopy12.30BM2-118[»]
4V48electron microscopy11.50BM2-118[»]
4V4HX-ray3.46AM/CM1-118[»]
4V4QX-ray3.46AM/CM2-118[»]
4V4Velectron microscopy15.00AM2-116[»]
4V4Welectron microscopy15.00AM2-116[»]
4V50X-ray3.22AM/CM2-118[»]
4V52X-ray3.21AM/CM2-118[»]
4V53X-ray3.54AM/CM2-118[»]
4V54X-ray3.30AM/CM2-118[»]
4V55X-ray4.00AM/CM2-118[»]
4V56X-ray3.93AM/CM2-118[»]
4V57X-ray3.50AM/CM2-118[»]
4V5BX-ray3.74BM/DM2-118[»]
4V5Helectron microscopy5.80AM2-114[»]
4V5YX-ray4.45AM/CM2-118[»]
4V64X-ray3.50AM/CM2-118[»]
4V65electron microscopy9.00AF1-118[»]
4V66electron microscopy9.00AF1-118[»]
4V69electron microscopy6.70AM2-114[»]
4V6CX-ray3.19AM/CM1-118[»]
4V6DX-ray3.81AM/CM1-118[»]
4V6EX-ray3.71AM/CM1-118[»]
4V6Kelectron microscopy8.25BQ1-118[»]
4V6Lelectron microscopy13.20AQ1-118[»]
4V6Nelectron microscopy12.10BP2-118[»]
4V6Oelectron microscopy14.70AP2-118[»]
4V6Pelectron microscopy13.50AP2-118[»]
4V6Qelectron microscopy11.50AP2-118[»]
4V6Relectron microscopy11.50AP2-118[»]
4V6Selectron microscopy13.10BO2-118[»]
4V6Telectron microscopy8.30AM2-115[»]
4V6Velectron microscopy9.80AM2-118[»]
4V6Yelectron microscopy12.00AM1-114[»]
4V6Zelectron microscopy12.00AM1-114[»]
4V70electron microscopy17.00AM1-114[»]
4V71electron microscopy20.00AM1-114[»]
4V72electron microscopy13.00AM1-114[»]
4V73electron microscopy15.00AM1-114[»]
4V74electron microscopy17.00AM1-114[»]
4V75electron microscopy12.00AM1-114[»]
4V76electron microscopy17.00AM1-114[»]
4V77electron microscopy17.00AM1-114[»]
4V78electron microscopy20.00AM1-114[»]
4V79electron microscopy15.00AM1-114[»]
4V7Aelectron microscopy9.00AM1-114[»]
4V7Belectron microscopy6.80AM1-118[»]
4V7Celectron microscopy7.60AM2-118[»]
4V7Delectron microscopy7.60BM2-118[»]
4V7Ielectron microscopy9.60BM1-118[»]
4V7SX-ray3.25AM2-115[»]
CM2-114[»]
4V7TX-ray3.19AM2-115[»]
CM2-114[»]
4V7UX-ray3.10AM/CM2-115[»]
4V7VX-ray3.29AM2-115[»]
CM2-114[»]
4V85X-ray3.20M1-118[»]
4V89X-ray3.70AM1-118[»]
4V9CX-ray3.30AM/CM1-118[»]
4V9DX-ray3.00AM/BM2-115[»]
4V9OX-ray2.90BM/DM/FM/HM1-118[»]
4V9PX-ray2.90BM/DM/FM/HM1-118[»]
4WF1X-ray3.09AM/CM2-115[»]
4WOIX-ray3.00AM/DM1-118[»]
4WWWX-ray3.10QM/XM2-115[»]
4YBBX-ray2.10AM/BM2-115[»]
5AFIelectron microscopy2.90m1-118[»]
5H5Uelectron microscopy3.00t2-118[»]
5IQRelectron microscopy3.00r1-118[»]
5IT8X-ray3.12AM/BM2-115[»]
5J5BX-ray2.80AM/BM2-115[»]
5J7LX-ray3.00AM/BM2-115[»]
5J88X-ray3.32AM/BM2-115[»]
5J8AX-ray3.10AM/BM2-115[»]
5J91X-ray2.96AM/BM2-115[»]
5JC9X-ray3.03AM/BM2-115[»]
5JTEelectron microscopy3.60AM1-118[»]
5JU8electron microscopy3.60AM1-118[»]
5KCRelectron microscopy3.601m1-118[»]
5KCSelectron microscopy3.901m1-118[»]
5KPSelectron microscopy3.90181-118[»]
5KPVelectron microscopy4.10171-118[»]
5KPWelectron microscopy3.90171-118[»]
5KPXelectron microscopy3.90171-118[»]
5L3Pelectron microscopy3.70m1-118[»]
5LZAelectron microscopy3.60m2-115[»]
5LZBelectron microscopy5.30m2-115[»]
5LZCelectron microscopy4.80m2-115[»]
5LZDelectron microscopy3.40m2-115[»]
5LZEelectron microscopy3.50m2-115[»]
5LZFelectron microscopy4.60m2-115[»]
5MDVelectron microscopy2.97r1-118[»]
5MDWelectron microscopy3.06r1-118[»]
5MDYelectron microscopy3.35r1-118[»]
5MDZelectron microscopy3.10r1-118[»]
5ME0electron microscopy13.50M1-118[»]
5ME1electron microscopy13.50M1-118[»]
5MGPelectron microscopy3.10m2-115[»]
5MY1electron microscopy7.60M2-118[»]
5NO2electron microscopy5.16M2-115[»]
5NO3electron microscopy5.16M2-115[»]
5NO4electron microscopy5.16M2-115[»]
5NP6electron microscopy3.60P2-115[»]
5NWYelectron microscopy2.93C1-118[»]
5O2Relectron microscopy3.40m2-115[»]
5U4Ielectron microscopy3.50m1-118[»]
5U9Felectron microscopy3.20M1-118[»]
5U9Gelectron microscopy3.20M1-118[»]
5UYKelectron microscopy3.90M2-115[»]
5UYLelectron microscopy3.60M2-115[»]
5UYMelectron microscopy3.20M2-115[»]
5UYNelectron microscopy4.00M2-115[»]
5UYPelectron microscopy3.90M2-115[»]
5UYQelectron microscopy3.80M2-115[»]
5UZ4electron microscopy5.80M1-118[»]
5WDTelectron microscopy3.00m2-116[»]
5WE4electron microscopy3.10m2-116[»]
5WE6electron microscopy3.40m2-115[»]
5WFKelectron microscopy3.40m2-116[»]
6BU8electron microscopy3.50M2-115[»]
6C4Ielectron microscopy3.24m1-118[»]
6DNCelectron microscopy3.70ZA1-118[»]
6ENFelectron microscopy3.20m2-115[»]
6ENJelectron microscopy3.70m2-115[»]
6ENUelectron microscopy3.10m2-115[»]
6GWTelectron microscopy3.80m2-115[»]
6GXMelectron microscopy3.80m2-115[»]
6GXNelectron microscopy3.90m2-115[»]
6GXOelectron microscopy3.90m2-115[»]
6GXPelectron microscopy4.40m2-115[»]
6H4Nelectron microscopy3.00m2-115[»]
6H58electron microscopy7.90m/mm2-115[»]
ProteinModelPortaliP0A7S9
SMRiP0A7S9
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35855N
IntActiP0A7S9, 108 interactors
STRINGi316385.ECDH10B_3473

Chemistry databases

DrugBankiDB00560 Tigecycline

Proteomic databases

EPDiP0A7S9
PaxDbiP0A7S9
PRIDEiP0A7S9

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76323; AAC76323; b3298
BAE77993; BAE77993; BAE77993
GeneIDi947791
KEGGiecj:JW3260
eco:b3298
PATRICifig|1411691.4.peg.3433

Organism-specific databases

EchoBASEiEB0905
EcoGeneiEG10912 rpsM

Phylogenomic databases

eggNOGiENOG4108Z04 Bacteria
COG0099 LUCA
HOGENOMiHOG000039879
InParanoidiP0A7S9
KOiK02952
PhylomeDBiP0A7S9

Enzyme and pathway databases

BioCyciEcoCyc:EG10912-MONOMER
MetaCyc:EG10912-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A7S9
PROiPR:P0A7S9

Family and domain databases

Gene3Di4.10.910.10, 1 hit
HAMAPiMF_01315 Ribosomal_S13_S18, 1 hit
InterProiView 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
PANTHERiPTHR10871:SF1 PTHR10871:SF1, 1 hit
PfamiView protein in Pfam
PF00416 Ribosomal_S13, 1 hit
PIRSFiPIRSF002134 Ribosomal_S13, 1 hit
SUPFAMiSSF46946 SSF46946, 1 hit
TIGRFAMsiTIGR03631 uS13_bact, 1 hit
PROSITEiView protein in PROSITE
PS00646 RIBOSOMAL_S13_1, 1 hit
PS50159 RIBOSOMAL_S13_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRS13_ECOLI
AccessioniPrimary (citable) accession number: P0A7S9
Secondary accession number(s): P02369, Q2M6W3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 139 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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