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P0A7W1

- RS5_ECOLI

UniProt

P0A7W1 - RS5_ECOLI

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Protein

30S ribosomal protein S5

Gene

rpsE

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: UniProtKB-HAMAP

GO - Biological processi

  1. response to antibiotic Source: UniProtKB-KW
  2. translation Source: UniProtKB-HAMAP
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
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10904. rpsE.

Subcellular locationi

GO - Cellular componenti

  1. 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 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

PaxDbiP0A7W1.
PRIDEiP0A7W1.

Expressioni

Gene expression databases

GenevestigatoriP0A7W1.

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

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[»]
1P6Gelectron microscopy12.30E2-167[»]
1P87electron microscopy11.50E2-167[»]
1VS5X-ray3.46E1-167[»]
1VS7X-ray3.46E1-167[»]
2AVYX-ray3.46E2-167[»]
2AW7X-ray3.46E2-167[»]
2GY9electron microscopy15.00E10-157[»]
2GYBelectron microscopy15.00E10-157[»]
2I2PX-ray3.22E2-167[»]
2I2UX-ray3.22E2-167[»]
2QALX-ray3.21E2-167[»]
2QANX-ray3.21E2-167[»]
2QB9X-ray3.54E2-167[»]
2QBBX-ray3.54E2-167[»]
2QBDX-ray3.30E2-167[»]
2QBFX-ray3.30E2-167[»]
2QBHX-ray4.00E2-167[»]
2QBJX-ray4.00E2-167[»]
2QOUX-ray3.93E2-167[»]
2QOWX-ray3.93E2-167[»]
2QOYX-ray3.50E2-167[»]
2QP0X-ray3.50E2-167[»]
2VHOX-ray3.74E2-167[»]
2VHPX-ray3.74E2-167[»]
2WWLelectron microscopy5.80E10-159[»]
2YKRelectron microscopy9.80E10-159[»]
2Z4KX-ray4.45E2-167[»]
2Z4MX-ray4.45E2-167[»]
3DF1X-ray3.50E2-167[»]
3DF3X-ray3.50E2-166[»]
3E1Aelectron microscopy-S1-159[»]
3E1Celectron microscopy-S1-159[»]
3FIHelectron microscopy6.70E10-159[»]
3I1MX-ray3.19E1-167[»]
3I1OX-ray3.19E1-167[»]
3I1QX-ray3.81E1-167[»]
3I1SX-ray3.81E1-167[»]
3I1ZX-ray3.71E1-167[»]
3I21X-ray3.71E1-167[»]
3IZVelectron microscopy-I1-167[»]
3IZWelectron microscopy-I1-167[»]
3J00electron microscopy-E2-167[»]
3J0Uelectron microscopy12.10H2-167[»]
3J0Velectron microscopy14.70H2-167[»]
3J0Xelectron microscopy13.50H2-167[»]
3J0Zelectron microscopy11.50H2-167[»]
3J10electron microscopy11.50H2-167[»]
3J13electron microscopy13.10G2-167[»]
3J18electron microscopy8.30E10-159[»]
3J36electron microscopy9.80E2-167[»]
3J4Velectron microscopy12.00E10-159[»]
3J4Welectron microscopy12.00E10-159[»]
3J4Yelectron microscopy17.00E10-159[»]
3J4Zelectron microscopy20.00E10-159[»]
3J53electron microscopy13.00E10-159[»]
3J55electron microscopy15.00E10-159[»]
3J57electron microscopy17.00E10-159[»]
3J59electron microscopy12.00E10-159[»]
3J5Belectron microscopy17.00E10-159[»]
3J5Delectron microscopy17.00E10-159[»]
3J5Felectron microscopy20.00E10-159[»]
3J5Helectron microscopy15.00E10-159[»]
3J5Jelectron microscopy9.00E10-159[»]
3J5Nelectron microscopy6.80E1-167[»]
3J5Telectron microscopy7.60E2-167[»]
3J5Xelectron microscopy7.60E2-167[»]
3KC4electron microscopy-E1-167[»]
3OAQX-ray3.25E10-159[»]
3OARX-ray3.25E10-159[»]
3OFAX-ray3.19E10-159[»]
3OFBX-ray3.19E10-159[»]
3OFOX-ray3.10E10-159[»]
3OFPX-ray3.10E10-159[»]
3OFXX-ray3.29E10-159[»]
3OFYX-ray3.29E10-159[»]
3OR9X-ray3.30E1-167[»]
3ORAX-ray3.30E1-167[»]
3SFSX-ray3.20E1-167[»]
3UOQX-ray3.70E1-167[»]
4A2Ielectron microscopy16.50E10-159[»]
4ADVelectron microscopy13.50E2-167[»]
4GAQX-ray3.30E1-167[»]
4GASX-ray3.30E1-167[»]
4GD1X-ray3.00E10-159[»]
4GD2X-ray3.00E10-159[»]
4KIYX-ray2.90E1-167[»]
4KJ0X-ray2.90E1-167[»]
4KJ2X-ray2.90E1-167[»]
4KJ4X-ray2.90E1-167[»]
4KJ6X-ray2.90E1-167[»]
4KJ8X-ray2.90E1-167[»]
4KJAX-ray2.90E1-167[»]
4KJCX-ray2.90E1-167[»]
4PE9X-ray2.95E10-159[»]
4PEAX-ray2.95E10-159[»]
4TOLX-ray3.00E10-159[»]
4TONX-ray3.00E10-159[»]
4TOUX-ray2.90E10-159[»]
4TOWX-ray2.90E10-159[»]
4TP0X-ray2.90E10-159[»]
4TP2X-ray2.90E10-159[»]
4TP4X-ray2.90E10-159[»]
4TP6X-ray2.90E10-159[»]
4TP8X-ray2.80E10-159[»]
4TPAX-ray2.80E10-159[»]
4TPCX-ray2.80E10-159[»]
4TPEX-ray2.80E10-159[»]
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.
HOGENOMiHOG000072595.
InParanoidiP0A7W1.
KOiK02988.
OMAiPAHEGTG.
OrthoDBiEOG6FJNM5.
PhylomeDBiP0A7W1.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
3.30.230.10. 1 hit.
HAMAPiMF_01307_B. Ribosomal_S5_B.
InterProiIPR014720. dsRNA-bd_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.
YP_492129.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76328; AAC76328; b3303.
BAE77988; BAE77988; BAE77988.
GeneIDi12934414.
947795.
KEGGiecj:Y75_p3873.
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 .
PIRi B65123. R3EC5.
RefSeqi NP_417762.1. NC_000913.3.
YP_492129.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EG0 electron microscopy 11.50 B 1-148 [» ]
1M5G model - E 10-159 [» ]
1P6G electron microscopy 12.30 E 2-167 [» ]
1P87 electron microscopy 11.50 E 2-167 [» ]
1VS5 X-ray 3.46 E 1-167 [» ]
1VS7 X-ray 3.46 E 1-167 [» ]
2AVY X-ray 3.46 E 2-167 [» ]
2AW7 X-ray 3.46 E 2-167 [» ]
2GY9 electron microscopy 15.00 E 10-157 [» ]
2GYB electron microscopy 15.00 E 10-157 [» ]
2I2P X-ray 3.22 E 2-167 [» ]
2I2U X-ray 3.22 E 2-167 [» ]
2QAL X-ray 3.21 E 2-167 [» ]
2QAN X-ray 3.21 E 2-167 [» ]
2QB9 X-ray 3.54 E 2-167 [» ]
2QBB X-ray 3.54 E 2-167 [» ]
2QBD X-ray 3.30 E 2-167 [» ]
2QBF X-ray 3.30 E 2-167 [» ]
2QBH X-ray 4.00 E 2-167 [» ]
2QBJ X-ray 4.00 E 2-167 [» ]
2QOU X-ray 3.93 E 2-167 [» ]
2QOW X-ray 3.93 E 2-167 [» ]
2QOY X-ray 3.50 E 2-167 [» ]
2QP0 X-ray 3.50 E 2-167 [» ]
2VHO X-ray 3.74 E 2-167 [» ]
2VHP X-ray 3.74 E 2-167 [» ]
2WWL electron microscopy 5.80 E 10-159 [» ]
2YKR electron microscopy 9.80 E 10-159 [» ]
2Z4K X-ray 4.45 E 2-167 [» ]
2Z4M X-ray 4.45 E 2-167 [» ]
3DF1 X-ray 3.50 E 2-167 [» ]
3DF3 X-ray 3.50 E 2-166 [» ]
3E1A electron microscopy - S 1-159 [» ]
3E1C electron microscopy - S 1-159 [» ]
3FIH electron microscopy 6.70 E 10-159 [» ]
3I1M X-ray 3.19 E 1-167 [» ]
3I1O X-ray 3.19 E 1-167 [» ]
3I1Q X-ray 3.81 E 1-167 [» ]
3I1S X-ray 3.81 E 1-167 [» ]
3I1Z X-ray 3.71 E 1-167 [» ]
3I21 X-ray 3.71 E 1-167 [» ]
3IZV electron microscopy - I 1-167 [» ]
3IZW electron microscopy - I 1-167 [» ]
3J00 electron microscopy - E 2-167 [» ]
3J0U electron microscopy 12.10 H 2-167 [» ]
3J0V electron microscopy 14.70 H 2-167 [» ]
3J0X electron microscopy 13.50 H 2-167 [» ]
3J0Z electron microscopy 11.50 H 2-167 [» ]
3J10 electron microscopy 11.50 H 2-167 [» ]
3J13 electron microscopy 13.10 G 2-167 [» ]
3J18 electron microscopy 8.30 E 10-159 [» ]
3J36 electron microscopy 9.80 E 2-167 [» ]
3J4V electron microscopy 12.00 E 10-159 [» ]
3J4W electron microscopy 12.00 E 10-159 [» ]
3J4Y electron microscopy 17.00 E 10-159 [» ]
3J4Z electron microscopy 20.00 E 10-159 [» ]
3J53 electron microscopy 13.00 E 10-159 [» ]
3J55 electron microscopy 15.00 E 10-159 [» ]
3J57 electron microscopy 17.00 E 10-159 [» ]
3J59 electron microscopy 12.00 E 10-159 [» ]
3J5B electron microscopy 17.00 E 10-159 [» ]
3J5D electron microscopy 17.00 E 10-159 [» ]
3J5F electron microscopy 20.00 E 10-159 [» ]
3J5H electron microscopy 15.00 E 10-159 [» ]
3J5J electron microscopy 9.00 E 10-159 [» ]
3J5N electron microscopy 6.80 E 1-167 [» ]
3J5T electron microscopy 7.60 E 2-167 [» ]
3J5X electron microscopy 7.60 E 2-167 [» ]
3KC4 electron microscopy - E 1-167 [» ]
3OAQ X-ray 3.25 E 10-159 [» ]
3OAR X-ray 3.25 E 10-159 [» ]
3OFA X-ray 3.19 E 10-159 [» ]
3OFB X-ray 3.19 E 10-159 [» ]
3OFO X-ray 3.10 E 10-159 [» ]
3OFP X-ray 3.10 E 10-159 [» ]
3OFX X-ray 3.29 E 10-159 [» ]
3OFY X-ray 3.29 E 10-159 [» ]
3OR9 X-ray 3.30 E 1-167 [» ]
3ORA X-ray 3.30 E 1-167 [» ]
3SFS X-ray 3.20 E 1-167 [» ]
3UOQ X-ray 3.70 E 1-167 [» ]
4A2I electron microscopy 16.50 E 10-159 [» ]
4ADV electron microscopy 13.50 E 2-167 [» ]
4GAQ X-ray 3.30 E 1-167 [» ]
4GAS X-ray 3.30 E 1-167 [» ]
4GD1 X-ray 3.00 E 10-159 [» ]
4GD2 X-ray 3.00 E 10-159 [» ]
4KIY X-ray 2.90 E 1-167 [» ]
4KJ0 X-ray 2.90 E 1-167 [» ]
4KJ2 X-ray 2.90 E 1-167 [» ]
4KJ4 X-ray 2.90 E 1-167 [» ]
4KJ6 X-ray 2.90 E 1-167 [» ]
4KJ8 X-ray 2.90 E 1-167 [» ]
4KJA X-ray 2.90 E 1-167 [» ]
4KJC X-ray 2.90 E 1-167 [» ]
4PE9 X-ray 2.95 E 10-159 [» ]
4PEA X-ray 2.95 E 10-159 [» ]
4TOL X-ray 3.00 E 10-159 [» ]
4TON X-ray 3.00 E 10-159 [» ]
4TOU X-ray 2.90 E 10-159 [» ]
4TOW X-ray 2.90 E 10-159 [» ]
4TP0 X-ray 2.90 E 10-159 [» ]
4TP2 X-ray 2.90 E 10-159 [» ]
4TP4 X-ray 2.90 E 10-159 [» ]
4TP6 X-ray 2.90 E 10-159 [» ]
4TP8 X-ray 2.80 E 10-159 [» ]
4TPA X-ray 2.80 E 10-159 [» ]
4TPC X-ray 2.80 E 10-159 [» ]
4TPE X-ray 2.80 E 10-159 [» ]
ProteinModelPortali P0A7W1.
SMRi P0A7W1. Positions 10-159.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10781N.
IntActi P0A7W1. 190 interactions.
MINTi MINT-6478202.
STRINGi 511145.b3303.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0A7W1.
PRIDEi P0A7W1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76328 ; AAC76328 ; b3303 .
BAE77988 ; BAE77988 ; BAE77988 .
GeneIDi 12934414.
947795.
KEGGi ecj:Y75_p3873.
eco:b3303.
PATRICi 32122038. VBIEscCol129921_3396.

Organism-specific databases

EchoBASEi EB0897.
EcoGenei EG10904. rpsE.

Phylogenomic databases

eggNOGi COG0098.
HOGENOMi HOG000072595.
InParanoidi P0A7W1.
KOi K02988.
OMAi PAHEGTG.
OrthoDBi EOG6FJNM5.
PhylomeDBi P0A7W1.

Enzyme and pathway databases

BioCyci EcoCyc:EG10904-MONOMER.
ECOL316407:JW3265-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7W1.
PROi P0A7W1.

Gene expression databases

Genevestigatori P0A7W1.

Family and domain databases

Gene3Di 3.30.160.20. 1 hit.
3.30.230.10. 1 hit.
HAMAPi MF_01307_B. Ribosomal_S5_B.
InterProi IPR014720. dsRNA-bd_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 ]
PANTHERi PTHR13718. PTHR13718. 1 hit.
Pfami PF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
TIGRFAMsi TIGR01021. rpsE_bact. 1 hit.
PROSITEi PS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
    Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
    Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The primary structure of protein S5 from the small subunit of the Escherichia coli ribosome."
    Wittmann-Liebold B., Greuer B.
    FEBS Lett. 95:91-98(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-167, ACETYLATION AT ALA-2, VARIANTS, MUTANTS.
    Strain: B and K.
  5. "Localization of the amino-acid exchange in protein S5 from an Escherichia coli mutant resistant to spectinomycin."
    DeWilde M., Wittmann-Liebold B.
    Mol. Gen. Genet. 127:273-276(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 15-23, VARIANT SPECTINOMYCIN RESISTANT.
    Strain: B.
  6. "Requirement of proteins S5 and S9 from 30S subunits for the ribosome-dependent GTPase activity of elongation factor G."
    Marsh R.C., Parmeggiani A.
    Proc. Natl. Acad. Sci. U.S.A. 70:151-155(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN FORMATION OF THE EF-G/RIBOSOME COMPLEX.
    Strain: B/2.
  7. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  8. "Ribosomal RNA and protein mutants resistant to spectinomycin."
    Bilgin N., Richter A.A., Ehrenberg M., Dahlberg A.E., Kurland C.G.
    EMBO J. 9:735-739(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS.
    Strain: O17.
  9. "The path of mRNA through the Escherichia coli ribosome; site-directed cross-linking of mRNA analogues carrying a photo-reactive label at various points 3' to the decoding site."
    Rinke-Appel J., Juenke N., Stade K., Brimacombe R.
    EMBO J. 10:2195-2202(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO MRNA.
  10. "mRNA helicase activity of the ribosome."
    Takyar S., Hickerson R.P., Noller H.F.
    Cell 120:49-58(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN MRNA HELICASE ACTIVITY, MUTAGENESIS.
    Strain: MRE-600.
  11. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  12. "All-atom homology model of the Escherichia coli 30S ribosomal subunit."
    Tung C.-S., Joseph S., Sanbonmatsu K.Y.
    Nat. Struct. Biol. 9:750-755(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  13. "Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
    Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
    Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
    Strain: MRE-600.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.
  15. "Limitations of translational accuracy."
    Kurland C.G., Hughes D., Ehrenberg M.
    (In) Neidhardt F.C., Curtiss R. III, Ingraham J.L., Lin E.C.C., Low K.B. Magasanik B., Reznikoff W.S., Riley M., Schaechter M., Umbarger H.E. (eds.); Escherichia coli and Salmonella: Cellular and molecular biology (2nd ed.), pp.979-1004, American Society for Microbiology Press, Washington D.C. (1996)
    Cited for: REVIEW ON TRANSLATIONAL ACCURACY.

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: November 26, 2014
This is version 109 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

External Data

Dasty 3