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Protein

30S ribosomal protein S5

Gene

rpsE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

GO - Molecular functioni

GO - Biological processi

  • maintenance of translational fidelity Source: EcoCyc
  • response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10904-MONOMER.
ECOL316407:JW3265-MONOMER.

Names & Taxonomyi

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

Organism-specific databases

EcoGeneiEG10904. rpsE.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic small ribosomal subunit Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 2910RVSKTVKGGR → AVSKTVKGGA: No effect on mRNA unwinding ability of the ribosome. 1 Publication

Chemistry

ChEMBLiCHEMBL2363135.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 16716630S ribosomal protein S5PRO_0000131511Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0A7W1.
PaxDbiP0A7W1.
PRIDEiP0A7W1.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. 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. Can be cross-linked to mRNA.

Binary interactionsi

WithEntry#Exp.IntActNotes
rnbP308502EBI-543949,EBI-557325
rplWP0ADZ02EBI-543949,EBI-542264

Protein-protein interaction databases

BioGridi4263408. 36 interactions.
DIPiDIP-10781N.
IntActiP0A7W1. 190 interactions.
MINTiMINT-6478202.
STRINGi511145.b3303.

Structurei

Secondary structure

1
167
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 2210Combined sources
Beta strandi26 – 283Combined sources
Beta strandi31 – 4010Combined sources
Beta strandi42 – 443Combined sources
Beta strandi46 – 494Combined sources
Beta strandi52 – 554Combined sources
Helixi56 – 6813Combined sources
Beta strandi69 – 724Combined sources
Beta strandi78 – 803Combined sources
Beta strandi85 – 895Combined sources
Beta strandi92 – 976Combined sources
Beta strandi101 – 1033Combined sources
Turni109 – 1113Combined sources
Helixi112 – 1187Combined sources
Beta strandi120 – 1234Combined sources
Beta strandi124 – 1296Combined sources
Helixi133 – 14614Combined sources
Helixi150 – 1523Combined sources
Helixi153 – 1564Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
5IQRelectron microscopy3.00j1-167[»]
ProteinModelPortaliP0A7W1.
SMRiP0A7W1. Positions 10-159.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7W1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 7464S5 DRBMAdd
BLAST

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

Belongs to the ribosomal protein S5P family.Curated
Contains 1 S5 DRBM domain.Curated

Phylogenomic databases

eggNOGiCOG0098. LUCA.
HOGENOMiHOG000072595.
InParanoidiP0A7W1.
KOiK02988.
OMAiPHEQKGK.
PhylomeDBiP0A7W1.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
3.30.230.10. 1 hit.
HAMAPiMF_01307_B. Ribosomal_S5_B. 1 hit.
InterProiIPR014720. dsRBD_dom.
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.
[Graphical view]
PANTHERiPTHR13718. PTHR13718. 1 hit.
PfamiPF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR01021. rpsE_bact. 1 hit.
PROSITEiPS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201R → L in strain: SPCR9; spectinomycin resistant. Not a ram mutation.
Natural varianti21 – 211V → E in strain: SPCR7; spectinomycin resistant. Not a ram mutation.
Natural varianti22 – 221S → P in strain: SPCR13 and SPCR15; spectinomycin resistant. Not a ram mutation.
Natural varianti104 – 1041G → R in strain: N-660; suppresses S12 streptomycin dependence.
Natural varianti112 – 1121R → G in strain: NEA-314; neamycin resistant.
Natural varianti112 – 1121R → L in strain: N-421 and D-1023; suppresses S12 streptomycin-dependence.
Natural varianti112 – 1121R → S in strain: NEA-319; neamycin resistant.
Natural varianti151 – 1511E → S in strain: B.
Natural varianti162 – 1676EEILGK → G in strain: 0-1; suppresses an alanyl-tRNA synthetase mutation. Blocks ribosome assembly below 25 degrees Celsius.

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.
PATRICi32122038. VBIEscCol129921_3396.

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
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[»]
5IQRelectron microscopy3.00j1-167[»]
ProteinModelPortaliP0A7W1.
SMRiP0A7W1. Positions 10-159.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263408. 36 interactions.
DIPiDIP-10781N.
IntActiP0A7W1. 190 interactions.
MINTiMINT-6478202.
STRINGi511145.b3303.

Chemistry

ChEMBLiCHEMBL2363135.

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.
PATRICi32122038. VBIEscCol129921_3396.

Organism-specific databases

EchoBASEiEB0897.
EcoGeneiEG10904. rpsE.

Phylogenomic databases

eggNOGiCOG0098. LUCA.
HOGENOMiHOG000072595.
InParanoidiP0A7W1.
KOiK02988.
OMAiPHEQKGK.
PhylomeDBiP0A7W1.

Enzyme and pathway databases

BioCyciEcoCyc:EG10904-MONOMER.
ECOL316407:JW3265-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7W1.
PROiP0A7W1.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
3.30.230.10. 1 hit.
HAMAPiMF_01307_B. Ribosomal_S5_B. 1 hit.
InterProiIPR014720. dsRBD_dom.
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.
[Graphical view]
PANTHERiPTHR13718. PTHR13718. 1 hit.
PfamiPF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR01021. rpsE_bact. 1 hit.
PROSITEiPS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRS5_ECOLI
AccessioniPrimary (citable) accession number: P0A7W1
Secondary accession number(s): O54299, P02356, Q2M6W8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.