Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

30S ribosomal protein S5

Gene

rpsE

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

Functioni

With S4 and S12 plays an important role in translational accuracy. Many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations).1 Publication
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.1 Publication
The physical location of this protein suggests it may also play a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp.1 Publication

Miscellaneous

Altered S5 proteins have been identified in a number of mutants. Some mutations in S5 have been shown to increase translational error frequencies.
Some mutants in this protein can partially suppress an alanyl-tRNA synthetase mutant.

GO - Molecular functioni

  • rRNA binding Source: UniProtKB-UniRule
  • structural constituent of ribosome Source: CAFA

GO - Biological processi

  • maintenance of translational fidelity Source: EcoCyc
  • response to antibiotic Source: UniProtKB-KW
  • ribosomal small subunit assembly Source: CAFA

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding
Biological processAntibiotic resistance

Enzyme and pathway databases

BioCyciEcoCyc:EG10904-MONOMER
MetaCyc:EG10904-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S5
Alternative name(s):
Small ribosomal subunit protein uS51 Publication
Gene namesi
Name:rpsE
Synonyms:spc
Ordered Locus Names:b3303, JW3265
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10904 rpsE

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi20 – 29RVSKTVKGGR → AVSKTVKGGA: No effect on mRNA unwinding ability of the ribosome. 1 Publication10

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001315112 – 16730S ribosomal protein S5Add BLAST166

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0A7W1
PaxDbiP0A7W1
PRIDEiP0A7W1

PTM databases

iPTMnetiP0A7W1

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit (PubMed:363452, PubMed:4273819, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:10094780, PubMed:12244297, PubMed:27906160, PubMed:27906161, PubMed:28077875). Contacts proteins S4 and S8. With proteins S4 and S5 encircles the mRNA as it enters the ribosome, which may play a role in mRNA helicase processivity (PubMed:15652481). Can be cross-linked to mRNA (PubMed:1712292).12 Publications

Binary interactionsi

Protein-protein interaction databases

BioGridi4263408, 155 interactors
DIPiDIP-10781N
IntActiP0A7W1, 193 interactors
MINTiP0A7W1
STRINGi316385.ECDH10B_3478

Structurei

Secondary structure

1167
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0A7W1
SMRiP0A7W1
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7W1

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 74S5 DRBMAdd BLAST64

Domaini

The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0098 LUCA
HOGENOMiHOG000072595
InParanoidiP0A7W1
KOiK02988
PhylomeDBiP0A7W1

Family and domain databases

Gene3Di3.30.230.10, 1 hit
HAMAPiMF_01307_B Ribosomal_S5_B, 1 hit
InterProiView protein in InterPro
IPR000851 Ribosomal_S5
IPR005712 Ribosomal_S5_bac-type
IPR005324 Ribosomal_S5_C
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR013810 Ribosomal_S5_N
IPR018192 Ribosomal_S5_N_CS
PANTHERiPTHR13718 PTHR13718, 1 hit
PfamiView protein in Pfam
PF00333 Ribosomal_S5, 1 hit
PF03719 Ribosomal_S5_C, 1 hit
SUPFAMiSSF54211 SSF54211, 1 hit
TIGRFAMsiTIGR01021 rpsE_bact, 1 hit
PROSITEiView protein in PROSITE
PS00585 RIBOSOMAL_S5, 1 hit
PS50881 S5_DSRBD, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0A7W1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAHIEKQAGE LQEKLIAVNR VSKTVKGGRI FSFTALTVVG DGNGRVGFGY
60 70 80 90 100
GKAREVPAAI QKAMEKARRN MINVALNNGT LQHPVKGVHT GSRVFMQPAS
110 120 130 140 150
EGTGIIAGGA MRAVLEVAGV HNVLAKAYGS TNPINVVRAT IDGLENMNSP
160
EMVAAKRGKS VEEILGK
Length:167
Mass (Da):17,603
Last modified:January 23, 2007 - v2
Checksum:i0B7EA2CB34018CAB
GO

Mass spectrometryi

Molecular mass is 17514.8 Da from positions 2 - 167. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti20R → L in strain: SPCR9; spectinomycin resistant. Not a ram mutation. 1
Natural varianti21V → E in strain: SPCR7; spectinomycin resistant. Not a ram mutation. 1
Natural varianti22S → P in strain: SPCR13 and SPCR15; spectinomycin resistant. Not a ram mutation. 1
Natural varianti104G → R in strain: N-660; suppresses S12 streptomycin dependence. 1
Natural varianti112R → G in strain: NEA-314; neamycin resistant. 1
Natural varianti112R → L in strain: N-421 and D-1023; suppresses S12 streptomycin-dependence. 1
Natural varianti112R → S in strain: NEA-319; neamycin resistant. 1
Natural varianti151E → S in strain: B. 1
Natural varianti162 – 167EEILGK → G in strain: 0-1; suppresses an alanyl-tRNA synthetase mutation. Blocks ribosome assembly below 25 degrees Celsius. 6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA Translation: CAA25722.1
U18997 Genomic DNA Translation: AAA58100.1
U00096 Genomic DNA Translation: AAC76328.1
AP009048 Genomic DNA Translation: BAE77988.1
PIRiB65123 R3EC5
RefSeqiNP_417762.1, NC_000913.3
WP_000940121.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76328; AAC76328; b3303
BAE77988; BAE77988; BAE77988
GeneIDi947795
KEGGiecj:JW3265
eco:b3303
PATRICifig|1411691.4.peg.3428

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA Translation: CAA25722.1
U18997 Genomic DNA Translation: AAA58100.1
U00096 Genomic DNA Translation: AAC76328.1
AP009048 Genomic DNA Translation: BAE77988.1
PIRiB65123 R3EC5
RefSeqiNP_417762.1, NC_000913.3
WP_000940121.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50B1-148[»]
1M5Gmodel-E10-159[»]
2YKRelectron microscopy9.80E10-159[»]
3J9Yelectron microscopy3.90e1-167[»]
3J9Zelectron microscopy3.60SE2-167[»]
3JA1electron microscopy3.60SE2-167[»]
3JBUelectron microscopy3.64E1-167[»]
3JBVelectron microscopy3.32E1-167[»]
3JCDelectron microscopy3.70e1-167[»]
3JCEelectron microscopy3.20e1-167[»]
3JCJelectron microscopy3.70k1-167[»]
3JCNelectron microscopy4.60f1-159[»]
4A2Ielectron microscopy16.50E10-159[»]
4ADVelectron microscopy13.50E2-167[»]
4U1UX-ray2.95AE/CE10-159[»]
4U1VX-ray3.00AE/CE10-159[»]
4U20X-ray2.90AE/CE10-159[»]
4U24X-ray2.90AE/CE10-159[»]
4U25X-ray2.90AE/CE10-159[»]
4U26X-ray2.80AE/CE10-159[»]
4U27X-ray2.80AE/CE10-159[»]
4V47electron microscopy12.30BE2-167[»]
4V48electron microscopy11.50BE2-167[»]
4V4HX-ray3.46AE/CE1-167[»]
4V4QX-ray3.46AE/CE2-167[»]
4V4Velectron microscopy15.00AE10-157[»]
4V4Welectron microscopy15.00AE10-157[»]
4V50X-ray3.22AE/CE2-167[»]
4V52X-ray3.21AE/CE2-167[»]
4V53X-ray3.54AE/CE2-167[»]
4V54X-ray3.30AE/CE2-167[»]
4V55X-ray4.00AE/CE2-167[»]
4V56X-ray3.93AE/CE2-167[»]
4V57X-ray3.50AE/CE2-167[»]
4V5BX-ray3.74BE/DE2-167[»]
4V5Helectron microscopy5.80AE10-159[»]
4V5YX-ray4.45AE/CE2-167[»]
4V64X-ray3.50AE/CE2-167[»]
4V65electron microscopy9.00AS1-159[»]
4V66electron microscopy9.00AS1-159[»]
4V69electron microscopy6.70AE10-159[»]
4V6CX-ray3.19AE/CE1-167[»]
4V6DX-ray3.81AE/CE1-167[»]
4V6EX-ray3.71AE/CE1-167[»]
4V6Kelectron microscopy8.25BI1-167[»]
4V6Lelectron microscopy13.20AI1-167[»]
4V6Melectron microscopy7.10AE2-167[»]
4V6Nelectron microscopy12.10BH2-167[»]
4V6Oelectron microscopy14.70AH2-167[»]
4V6Pelectron microscopy13.50AH2-167[»]
4V6Qelectron microscopy11.50AH2-167[»]
4V6Relectron microscopy11.50AH2-167[»]
4V6Selectron microscopy13.10BG2-167[»]
4V6Telectron microscopy8.30AE10-159[»]
4V6Velectron microscopy9.80AE2-167[»]
4V6Yelectron microscopy12.00AE10-159[»]
4V6Zelectron microscopy12.00AE10-159[»]
4V70electron microscopy17.00AE10-159[»]
4V71electron microscopy20.00AE10-159[»]
4V72electron microscopy13.00AE10-159[»]
4V73electron microscopy15.00AE10-159[»]
4V74electron microscopy17.00AE10-159[»]
4V75electron microscopy12.00AE10-159[»]
4V76electron microscopy17.00AE10-159[»]
4V77electron microscopy17.00AE10-159[»]
4V78electron microscopy20.00AE10-159[»]
4V79electron microscopy15.00AE10-159[»]
4V7Aelectron microscopy9.00AE10-159[»]
4V7Belectron microscopy6.80AE1-167[»]
4V7Celectron microscopy7.60AE2-167[»]
4V7Delectron microscopy7.60BE2-167[»]
4V7Ielectron microscopy9.60BE1-167[»]
4V7SX-ray3.25AE/CE10-159[»]
4V7TX-ray3.19AE/CE10-159[»]
4V7UX-ray3.10AE/CE10-159[»]
4V7VX-ray3.29AE/CE10-159[»]
4V85X-ray3.20E1-167[»]
4V89X-ray3.70AE1-167[»]
4V9CX-ray3.30AE/CE1-167[»]
4V9DX-ray3.00AE/BE10-159[»]
4V9OX-ray2.90BE/DE/FE/HE1-167[»]
4V9PX-ray2.90BE/DE/FE/HE1-167[»]
4WF1X-ray3.09AE/CE10-159[»]
4WOIX-ray3.00AE/DE1-167[»]
4WWWX-ray3.10QE/XE10-159[»]
4YBBX-ray2.10AE/BE10-164[»]
5AFIelectron microscopy2.90e1-167[»]
5H5Uelectron microscopy3.00l2-167[»]
5IQRelectron microscopy3.00j1-167[»]
5IT8X-ray3.12AE/BE10-164[»]
5J5BX-ray2.80AE/BE10-164[»]
5J7LX-ray3.00AE/BE10-164[»]
5J88X-ray3.32AE/BE10-164[»]
5J8AX-ray3.10AE/BE10-164[»]
5J91X-ray2.96AE/BE10-164[»]
5JC9X-ray3.03AE/BE10-164[»]
5JTEelectron microscopy3.60AE1-167[»]
5JU8electron microscopy3.60AE1-167[»]
5KCRelectron microscopy3.601e1-167[»]
5KCSelectron microscopy3.901e1-167[»]
5KPSelectron microscopy3.90101-167[»]
5KPVelectron microscopy4.1091-167[»]
5KPWelectron microscopy3.9091-167[»]
5KPXelectron microscopy3.9091-167[»]
5L3Pelectron microscopy3.70e1-167[»]
5LZAelectron microscopy3.60e10-166[»]
5LZBelectron microscopy5.30e10-166[»]
5LZCelectron microscopy4.80e10-166[»]
5LZDelectron microscopy3.40e10-166[»]
5LZEelectron microscopy3.50e10-166[»]
5LZFelectron microscopy4.60e10-166[»]
5MDVelectron microscopy2.97j1-167[»]
5MDWelectron microscopy3.06j1-167[»]
5MDYelectron microscopy3.35j1-167[»]
5MDZelectron microscopy3.10j1-167[»]
5ME0electron microscopy13.50E1-167[»]
5ME1electron microscopy13.50E1-167[»]
5MGPelectron microscopy3.10e10-166[»]
5MY1electron microscopy7.60E2-167[»]
5NO2electron microscopy5.16E10-164[»]
5NO3electron microscopy5.16E10-164[»]
5NO4electron microscopy5.16E10-164[»]
5NP6electron microscopy3.60H10-166[»]
5NWYelectron microscopy2.9341-166[»]
5O2Relectron microscopy3.40e10-166[»]
5U4Ielectron microscopy3.50e1-167[»]
5U4Jelectron microscopy3.70e1-167[»]
5U9Felectron microscopy3.20E1-167[»]
5U9Gelectron microscopy3.20E1-167[»]
5UYKelectron microscopy3.90E10-166[»]
5UYLelectron microscopy3.60E10-166[»]
5UYMelectron microscopy3.20E10-166[»]
5UYNelectron microscopy4.00E10-166[»]
5UYPelectron microscopy3.90E10-166[»]
5UYQelectron microscopy3.80E10-166[»]
5UZ4electron microscopy5.80E1-167[»]
5WDTelectron microscopy3.00e10-166[»]
5WE4electron microscopy3.10e10-166[»]
5WE6electron microscopy3.40e10-166[»]
5WFKelectron microscopy3.40e10-166[»]
6BU8electron microscopy3.50E10-166[»]
6C4Ielectron microscopy3.24e1-167[»]
6DNCelectron microscopy3.70RA1-167[»]
6ENFelectron microscopy3.20e10-166[»]
6ENJelectron microscopy3.70e10-166[»]
6ENUelectron microscopy3.10e10-166[»]
6GWTelectron microscopy3.80e10-166[»]
6GXMelectron microscopy3.80e10-166[»]
6GXNelectron microscopy3.90e10-166[»]
6GXOelectron microscopy3.90e10-166[»]
6GXPelectron microscopy4.40e10-166[»]
6H4Nelectron microscopy3.00e10-166[»]
6H58electron microscopy7.90e/ee10-166[»]
ProteinModelPortaliP0A7W1
SMRiP0A7W1
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263408, 155 interactors
DIPiDIP-10781N
IntActiP0A7W1, 193 interactors
MINTiP0A7W1
STRINGi316385.ECDH10B_3478

PTM databases

iPTMnetiP0A7W1

Proteomic databases

EPDiP0A7W1
PaxDbiP0A7W1
PRIDEiP0A7W1

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76328; AAC76328; b3303
BAE77988; BAE77988; BAE77988
GeneIDi947795
KEGGiecj:JW3265
eco:b3303
PATRICifig|1411691.4.peg.3428

Organism-specific databases

EchoBASEiEB0897
EcoGeneiEG10904 rpsE

Phylogenomic databases

eggNOGiCOG0098 LUCA
HOGENOMiHOG000072595
InParanoidiP0A7W1
KOiK02988
PhylomeDBiP0A7W1

Enzyme and pathway databases

BioCyciEcoCyc:EG10904-MONOMER
MetaCyc:EG10904-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A7W1
PROiPR:P0A7W1

Family and domain databases

Gene3Di3.30.230.10, 1 hit
HAMAPiMF_01307_B Ribosomal_S5_B, 1 hit
InterProiView protein in InterPro
IPR000851 Ribosomal_S5
IPR005712 Ribosomal_S5_bac-type
IPR005324 Ribosomal_S5_C
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR013810 Ribosomal_S5_N
IPR018192 Ribosomal_S5_N_CS
PANTHERiPTHR13718 PTHR13718, 1 hit
PfamiView protein in Pfam
PF00333 Ribosomal_S5, 1 hit
PF03719 Ribosomal_S5_C, 1 hit
SUPFAMiSSF54211 SSF54211, 1 hit
TIGRFAMsiTIGR01021 rpsE_bact, 1 hit
PROSITEiView protein in PROSITE
PS00585 RIBOSOMAL_S5, 1 hit
PS50881 S5_DSRBD, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRS5_ECOLI
AccessioniPrimary (citable) accession number: P0A7W1
Secondary accession number(s): O54299, P02356, Q2M6W8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 144 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again