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Protein

30S ribosomal protein S18

Gene

rpsR

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

Functioni

Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciEcoCyc:EG10917-MONOMER
MetaCyc:EG10917-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S18
Alternative name(s):
Small ribosomal subunit protein bS181 Publication
Gene namesi
Name:rpsR
Ordered Locus Names:b4202, JW4160
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10917 rpsR

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2363090

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001111532 – 7530S ribosomal protein S18Add BLAST74

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0A7T7
PaxDbiP0A7T7
PRIDEiP0A7T7

PTM databases

iPTMnetiP0A7T7

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit (PubMed:776663, PubMed:7556101, PubMed:10094780, PubMed:12244297, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:27906160, PubMed:27906161). Forms a tight heterodimer with protein S6.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
rpsFP023584EBI-548844,EBI-543068

Protein-protein interaction databases

DIPiDIP-47889N
IntActiP0A7T7, 29 interactors
STRINGi316385.ECDH10B_4397

Structurei

Secondary structure

175
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

DisProtiDP00146
ProteinModelPortaliP0A7T7
SMRiP0A7T7
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7T7

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0238 LUCA
HOGENOMiHOG000218466
InParanoidiP0A7T7
KOiK02963
PhylomeDBiP0A7T7

Family and domain databases

Gene3Di4.10.640.10, 1 hit
HAMAPiMF_00270 Ribosomal_S18, 1 hit
InterProiView protein in InterPro
IPR001648 Ribosomal_S18
IPR018275 Ribosomal_S18_CS
IPR036870 Ribosomal_S18_sf
PfamiView protein in Pfam
PF01084 Ribosomal_S18, 1 hit
PRINTSiPR00974 RIBOSOMALS18
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002239 Ribosomal_S18, 1 hit
SUPFAMiSSF46911 SSF46911, 1 hit
TIGRFAMsiTIGR00165 S18, 1 hit
PROSITEiView protein in PROSITE
PS00057 RIBOSOMAL_S18, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0A7T7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARYFRRRKF CRFTAEGVQE IDYKDIATLK NYITESGKIV PSRITGTRAK
60 70
YQRQLARAIK RARYLSLLPY TDRHQ
Length:75
Mass (Da):8,986
Last modified:January 23, 2007 - v2
Checksum:iAB2E8288901B73B8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti24K → E AA sequence (PubMed:776663).Curated1

Mass spectrometryi

Molecular mass is 8897.0 Da from positions 2 - 75. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04022 Genomic DNA Translation: CAA27654.1
U14003 Genomic DNA Translation: AAA97098.1
U00096 Genomic DNA Translation: AAC77159.1
AP009048 Genomic DNA Translation: BAE78203.1
PIRiS56427 R3EC18
RefSeqiNP_418623.1, NC_000913.3
WP_000135199.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC77159; AAC77159; b4202
BAE78203; BAE78203; BAE78203
GeneIDi948721
9735149
KEGGiecj:JW4160
eco:b4202
PATRICifig|1411691.4.peg.2499

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04022 Genomic DNA Translation: CAA27654.1
U14003 Genomic DNA Translation: AAA97098.1
U00096 Genomic DNA Translation: AAC77159.1
AP009048 Genomic DNA Translation: BAE78203.1
PIRiS56427 R3EC18
RefSeqiNP_418623.1, NC_000913.3
WP_000135199.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-R5-75[»]
2YKRelectron microscopy9.80R20-74[»]
3J9Yelectron microscopy3.90r1-75[»]
3J9Zelectron microscopy3.60SR2-75[»]
3JA1electron microscopy3.60SR2-75[»]
3JBUelectron microscopy3.64R1-75[»]
3JBVelectron microscopy3.32R1-75[»]
3JCDelectron microscopy3.70r1-75[»]
3JCEelectron microscopy3.20r1-75[»]
3JCJelectron microscopy3.7011-75[»]
3JCNelectron microscopy4.60u1-75[»]
4A2Ielectron microscopy16.50R20-74[»]
4ADVelectron microscopy13.50R2-75[»]
4U1UX-ray2.95AR/CR20-74[»]
4U1VX-ray3.00AR/CR20-74[»]
4U20X-ray2.90AR/CR20-74[»]
4U24X-ray2.90AR/CR20-74[»]
4U25X-ray2.90AR/CR20-74[»]
4U26X-ray2.80AR/CR20-74[»]
4U27X-ray2.80AR/CR20-74[»]
4V47electron microscopy12.30BR2-75[»]
4V48electron microscopy11.50BR2-75[»]
4V4HX-ray3.46AR/CR1-75[»]
4V4QX-ray3.46AR/CR2-75[»]
4V4Velectron microscopy15.00AR7-75[»]
4V4Welectron microscopy15.00AR7-75[»]
4V50X-ray3.22AR/CR2-75[»]
4V52X-ray3.21AR/CR2-75[»]
4V53X-ray3.54AR/CR2-75[»]
4V54X-ray3.30AR/CR2-75[»]
4V55X-ray4.00AR/CR2-75[»]
4V56X-ray3.93AR/CR2-75[»]
4V57X-ray3.50AR/CR2-75[»]
4V5BX-ray3.74BR/DR2-75[»]
4V5Helectron microscopy5.80AR20-74[»]
4V5YX-ray4.45AR/CR2-75[»]
4V64X-ray3.50AR/CR2-75[»]
4V65electron microscopy9.00AK1-75[»]
4V66electron microscopy9.00AK1-75[»]
4V69electron microscopy6.70AR20-74[»]
4V6CX-ray3.19AR/CR1-75[»]
4V6DX-ray3.81AR/CR1-75[»]
4V6EX-ray3.71AR/CR1-75[»]
4V6Kelectron microscopy8.25BV1-75[»]
4V6Lelectron microscopy13.20AV1-75[»]
4V6Melectron microscopy7.10AR2-75[»]
4V6Nelectron microscopy12.10BU2-75[»]
4V6Oelectron microscopy14.70AU2-75[»]
4V6Pelectron microscopy13.50AU2-75[»]
4V6Qelectron microscopy11.50AU2-75[»]
4V6Relectron microscopy11.50AU2-75[»]
4V6Selectron microscopy13.10BT2-75[»]
4V6Telectron microscopy8.30AR20-74[»]
4V6Velectron microscopy9.80AR2-75[»]
4V6Yelectron microscopy12.00AR20-74[»]
4V6Zelectron microscopy12.00AR20-74[»]
4V70electron microscopy17.00AR20-74[»]
4V71electron microscopy20.00AR20-74[»]
4V72electron microscopy13.00AR20-74[»]
4V73electron microscopy15.00AR20-74[»]
4V74electron microscopy17.00AR20-74[»]
4V75electron microscopy12.00AR20-74[»]
4V76electron microscopy17.00AR20-74[»]
4V77electron microscopy17.00AR20-74[»]
4V78electron microscopy20.00AR20-74[»]
4V79electron microscopy15.00AR20-74[»]
4V7Aelectron microscopy9.00AR20-74[»]
4V7Belectron microscopy6.80AR1-75[»]
4V7Celectron microscopy7.60AR2-75[»]
4V7Delectron microscopy7.60BR2-75[»]
4V7Ielectron microscopy9.60BR1-75[»]
4V7SX-ray3.25AR/CR20-74[»]
4V7TX-ray3.19AR/CR20-74[»]
4V7UX-ray3.10AR/CR20-74[»]
4V7VX-ray3.29AR/CR20-74[»]
4V85X-ray3.20R1-75[»]
4V89X-ray3.70AR1-75[»]
4V9CX-ray3.30AR/CR1-75[»]
4V9DX-ray3.00AR/BR20-74[»]
4V9OX-ray2.90BR/DR/FR/HR1-75[»]
4V9PX-ray2.90BR/DR/FR/HR1-75[»]
4WF1X-ray3.09AR/CR20-74[»]
4WOIX-ray3.00AR/DR1-75[»]
4WWWX-ray3.10QR/XR20-74[»]
4YBBX-ray2.10AR/BR20-74[»]
5AFIelectron microscopy2.90r1-75[»]
5H5Uelectron microscopy3.00y2-75[»]
5IQRelectron microscopy3.00w1-75[»]
5IT8X-ray3.12AR/BR20-74[»]
5J5BX-ray2.80AR/BR20-74[»]
5J7LX-ray3.00AR/BR20-74[»]
5J88X-ray3.32AR/BR20-74[»]
5J8AX-ray3.10AR/BR20-74[»]
5J91X-ray2.96AR/BR20-74[»]
5JC9X-ray3.03AR/BR20-74[»]
5JTEelectron microscopy3.60AR1-75[»]
5JU8electron microscopy3.60AR1-75[»]
5KCRelectron microscopy3.601r1-75[»]
5KCSelectron microscopy3.901r1-75[»]
5KPSelectron microscopy3.90231-75[»]
5KPVelectron microscopy4.10221-75[»]
5KPWelectron microscopy3.90221-75[»]
5KPXelectron microscopy3.90221-75[»]
5L3Pelectron microscopy3.70r1-75[»]
5LZAelectron microscopy3.60r10-74[»]
5LZBelectron microscopy5.30r10-74[»]
5LZCelectron microscopy4.80r10-74[»]
5LZDelectron microscopy3.40r10-74[»]
5LZEelectron microscopy3.50r10-74[»]
5LZFelectron microscopy4.60r10-74[»]
5MDVelectron microscopy2.97w1-75[»]
5MDWelectron microscopy3.06w1-75[»]
5MDYelectron microscopy3.35w1-75[»]
5MDZelectron microscopy3.10w1-75[»]
5ME0electron microscopy13.50R1-75[»]
5ME1electron microscopy13.50R1-75[»]
5MGPelectron microscopy3.10r10-74[»]
5MY1electron microscopy7.60R2-75[»]
5NO2electron microscopy5.16R20-74[»]
5NO3electron microscopy5.16R20-74[»]
5NO4electron microscopy5.16R20-74[»]
5NP6electron microscopy3.60U10-74[»]
5NWYelectron microscopy2.93H1-75[»]
5O2Relectron microscopy3.40r10-74[»]
5U4Ielectron microscopy3.50r1-75[»]
5U9Felectron microscopy3.20R1-75[»]
5U9Gelectron microscopy3.20R1-75[»]
5UYKelectron microscopy3.90R10-74[»]
5UYLelectron microscopy3.60R10-74[»]
5UYMelectron microscopy3.20R10-74[»]
5UYNelectron microscopy4.00R10-74[»]
5UYPelectron microscopy3.90R10-74[»]
5UYQelectron microscopy3.80R10-74[»]
5WDTelectron microscopy3.00r10-74[»]
5WE4electron microscopy3.10r10-74[»]
5WE6electron microscopy3.40r10-74[»]
5WFKelectron microscopy3.40r10-74[»]
6BU8electron microscopy3.50R10-74[»]
6C4Ielectron microscopy3.24r10-75[»]
6ENFelectron microscopy3.20r10-74[»]
6ENJelectron microscopy3.70r10-74[»]
6ENUelectron microscopy3.10r10-74[»]
6GWTelectron microscopy3.80r10-74[»]
6GXMelectron microscopy3.80r10-74[»]
6GXNelectron microscopy3.90r10-74[»]
6GXOelectron microscopy3.90r10-74[»]
6GXPelectron microscopy4.40r10-74[»]
6H4Nelectron microscopy3.00r10-74[»]
6H58electron microscopy7.90r/rr10-74[»]
DisProtiDP00146
ProteinModelPortaliP0A7T7
SMRiP0A7T7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47889N
IntActiP0A7T7, 29 interactors
STRINGi316385.ECDH10B_4397

Chemistry databases

ChEMBLiCHEMBL2363090

PTM databases

iPTMnetiP0A7T7

Proteomic databases

EPDiP0A7T7
PaxDbiP0A7T7
PRIDEiP0A7T7

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77159; AAC77159; b4202
BAE78203; BAE78203; BAE78203
GeneIDi948721
9735149
KEGGiecj:JW4160
eco:b4202
PATRICifig|1411691.4.peg.2499

Organism-specific databases

EchoBASEiEB0910
EcoGeneiEG10917 rpsR

Phylogenomic databases

eggNOGiCOG0238 LUCA
HOGENOMiHOG000218466
InParanoidiP0A7T7
KOiK02963
PhylomeDBiP0A7T7

Enzyme and pathway databases

BioCyciEcoCyc:EG10917-MONOMER
MetaCyc:EG10917-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A7T7
PROiPR:P0A7T7

Family and domain databases

Gene3Di4.10.640.10, 1 hit
HAMAPiMF_00270 Ribosomal_S18, 1 hit
InterProiView protein in InterPro
IPR001648 Ribosomal_S18
IPR018275 Ribosomal_S18_CS
IPR036870 Ribosomal_S18_sf
PfamiView protein in Pfam
PF01084 Ribosomal_S18, 1 hit
PRINTSiPR00974 RIBOSOMALS18
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002239 Ribosomal_S18, 1 hit
SUPFAMiSSF46911 SSF46911, 1 hit
TIGRFAMsiTIGR00165 S18, 1 hit
PROSITEiView protein in PROSITE
PS00057 RIBOSOMAL_S18, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRS18_ECOLI
AccessioniPrimary (citable) accession number: P0A7T7
Secondary accession number(s): P02374, Q2M6A3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 138 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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