UniProtKB - P0A7W1 (RS5_ECOLI)
Protein
30S ribosomal protein S5
Gene
rpsE
Organism
Escherichia coli (strain K12)
Status
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
- translation Source: GO_Central
Keywordsi
Molecular function | Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding |
Biological process | Antibiotic resistance |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10904-MONOMER MetaCyc:EG10904-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: 30S ribosomal protein S5Alternative name(s): Small ribosomal subunit protein uS51 Publication |
Gene namesi | Name:rpsE Synonyms:spc Ordered Locus Names:b3303, JW3265 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 20 – 29 | RVSKTVKGGR → AVSKTVKGGA: No effect on mRNA unwinding ability of the ribosome. 1 Publication | 10 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000131511 | 2 – 167 | 30S ribosomal protein S5Add BLAST | 166 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanine1 Publication | 1 |
Keywords - PTMi
AcetylationProteomic databases
jPOSTi | P0A7W1 |
PaxDbi | P0A7W1 |
PRIDEi | P0A7W1 |
PTM databases
iPTMneti | P0A7W1 |
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 PublicationsBinary interactionsi
Hide detailsP0A7W1
With | #Exp. | IntAct |
---|---|---|
lexA [P0A7C2] | 2 | EBI-543949,EBI-553416 |
rnb [P30850] | 3 | EBI-543949,EBI-557325 |
rplW [P0ADZ0] | 2 | EBI-543949,EBI-542264 |
Protein-protein interaction databases
BioGRIDi | 4263408, 155 interactors 852107, 3 interactors |
ComplexPortali | CPX-3802, 30S small ribosomal subunit |
DIPi | DIP-10781N |
IntActi | P0A7W1, 193 interactors |
MINTi | P0A7W1 |
STRINGi | 511145.b3303 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A7W1 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A7W1 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 11 – 74 | S5 DRBMAdd BLAST | 64 |
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 universal ribosomal protein uS5 family.Curated
Phylogenomic databases
eggNOGi | COG0098, Bacteria |
HOGENOMi | CLU_065898_2_2_6 |
InParanoidi | P0A7W1 |
PhylomeDBi | P0A7W1 |
Family and domain databases
Gene3Di | 3.30.230.10, 1 hit |
HAMAPi | MF_01307_B, Ribosomal_S5_B, 1 hit |
InterProi | View 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 |
PANTHERi | PTHR13718, PTHR13718, 1 hit |
Pfami | View protein in Pfam PF00333, Ribosomal_S5, 1 hit PF03719, Ribosomal_S5_C, 1 hit |
SUPFAMi | SSF54211, SSF54211, 1 hit |
TIGRFAMsi | TIGR01021, rpsE_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00585, RIBOSOMAL_S5, 1 hit PS50881, S5_DSRBD, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0A7W1-1 [UniParc]FASTAAdd to basket
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
Mass spectrometryi
Molecular mass is 17514.8 Da. Determined by MALDI. 1 Publication
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 20 | R → L in strain: SPCR9; spectinomycin resistant. Not a ram mutation. | 1 | |
Natural varianti | 21 | V → E in strain: SPCR7; spectinomycin resistant. Not a ram mutation. | 1 | |
Natural varianti | 22 | S → P in strain: SPCR13 and SPCR15; spectinomycin resistant. Not a ram mutation. | 1 | |
Natural varianti | 104 | G → R in strain: N-660; suppresses S12 streptomycin dependence. | 1 | |
Natural varianti | 112 | R → G in strain: NEA-314; neamycin resistant. | 1 | |
Natural varianti | 112 | R → L in strain: N-421 and D-1023; suppresses S12 streptomycin-dependence. | 1 | |
Natural varianti | 112 | R → S in strain: NEA-319; neamycin resistant. | 1 | |
Natural varianti | 151 | E → S in strain: B. | 1 | |
Natural varianti | 162 – 167 | EEILGK → 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 |
PIRi | B65123, R3EC5 |
RefSeqi | NP_417762.1, NC_000913.3 WP_000940121.1, NZ_STEB01000038.1 |
Genome annotation databases
EnsemblBacteriai | AAC76328; AAC76328; b3303 BAE77988; BAE77988; BAE77988 |
GeneIDi | 58463228 947795 |
KEGGi | ecj:JW3265 eco:b3303 |
PATRICi | fig|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 |
PIRi | B65123, R3EC5 |
RefSeqi | NP_417762.1, NC_000913.3 WP_000940121.1, NZ_STEB01000038.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1EG0 | electron microscopy | 11.50 | B | 1-148 | [»] | |
1M5G | model | - | E | 10-159 | [»] | |
2YKR | electron microscopy | 9.80 | E | 10-159 | [»] | |
3J9Y | electron microscopy | 3.90 | e | 1-167 | [»] | |
3J9Z | electron microscopy | 3.60 | SE | 2-167 | [»] | |
3JA1 | electron microscopy | 3.60 | SE | 2-167 | [»] | |
3JBU | electron microscopy | 3.64 | E | 1-167 | [»] | |
3JBV | electron microscopy | 3.32 | E | 1-167 | [»] | |
3JCD | electron microscopy | 3.70 | e | 1-167 | [»] | |
3JCE | electron microscopy | 3.20 | e | 1-167 | [»] | |
3JCJ | electron microscopy | 3.70 | k | 1-167 | [»] | |
3JCN | electron microscopy | 4.60 | f | 1-159 | [»] | |
4A2I | electron microscopy | 16.50 | E | 10-159 | [»] | |
4ADV | electron microscopy | 13.50 | E | 2-167 | [»] | |
4U1U | X-ray | 2.95 | AE/CE | 10-159 | [»] | |
4U1V | X-ray | 3.00 | AE/CE | 10-159 | [»] | |
4U20 | X-ray | 2.90 | AE/CE | 10-159 | [»] | |
4U24 | X-ray | 2.90 | AE/CE | 10-159 | [»] | |
4U25 | X-ray | 2.90 | AE/CE | 10-159 | [»] | |
4U26 | X-ray | 2.80 | AE/CE | 10-159 | [»] | |
4U27 | X-ray | 2.80 | AE/CE | 10-159 | [»] | |
4V47 | electron microscopy | 12.30 | BE | 2-167 | [»] | |
4V48 | electron microscopy | 11.50 | BE | 2-167 | [»] | |
4V4H | X-ray | 3.46 | AE/CE | 1-167 | [»] | |
4V4Q | X-ray | 3.46 | AE/CE | 2-167 | [»] | |
4V4V | electron microscopy | 15.00 | AE | 10-157 | [»] | |
4V4W | electron microscopy | 15.00 | AE | 10-157 | [»] | |
4V50 | X-ray | 3.22 | AE/CE | 2-167 | [»] | |
4V52 | X-ray | 3.21 | AE/CE | 2-167 | [»] | |
4V53 | X-ray | 3.54 | AE/CE | 2-167 | [»] | |
4V54 | X-ray | 3.30 | AE/CE | 2-167 | [»] | |
4V55 | X-ray | 4.00 | AE/CE | 2-167 | [»] | |
4V56 | X-ray | 3.93 | AE/CE | 2-167 | [»] | |
4V57 | X-ray | 3.50 | AE/CE | 2-167 | [»] | |
4V5B | X-ray | 3.74 | BE/DE | 2-167 | [»] | |
4V5H | electron microscopy | 5.80 | AE | 10-159 | [»] | |
4V5Y | X-ray | 4.45 | AE/CE | 2-167 | [»] | |
4V64 | X-ray | 3.50 | AE/CE | 2-167 | [»] | |
4V65 | electron microscopy | 9.00 | AS | 1-159 | [»] | |
4V66 | electron microscopy | 9.00 | AS | 1-159 | [»] | |
4V69 | electron microscopy | 6.70 | AE | 10-159 | [»] | |
4V6C | X-ray | 3.19 | AE/CE | 1-167 | [»] | |
4V6D | X-ray | 3.81 | AE/CE | 1-167 | [»] | |
4V6E | X-ray | 3.71 | AE/CE | 1-167 | [»] | |
4V6K | electron microscopy | 8.25 | BI | 1-167 | [»] | |
4V6L | electron microscopy | 13.20 | AI | 1-167 | [»] | |
4V6M | electron microscopy | 7.10 | AE | 2-167 | [»] | |
4V6N | electron microscopy | 12.10 | BH | 2-167 | [»] | |
4V6O | electron microscopy | 14.70 | AH | 2-167 | [»] | |
4V6P | electron microscopy | 13.50 | AH | 2-167 | [»] | |
4V6Q | electron microscopy | 11.50 | AH | 2-167 | [»] | |
4V6R | electron microscopy | 11.50 | AH | 2-167 | [»] | |
4V6S | electron microscopy | 13.10 | BG | 2-167 | [»] | |
4V6T | electron microscopy | 8.30 | AE | 10-159 | [»] | |
4V6V | electron microscopy | 9.80 | AE | 2-167 | [»] | |
4V6Y | electron microscopy | 12.00 | AE | 10-159 | [»] | |
4V6Z | electron microscopy | 12.00 | AE | 10-159 | [»] | |
4V70 | electron microscopy | 17.00 | AE | 10-159 | [»] | |
4V71 | electron microscopy | 20.00 | AE | 10-159 | [»] | |
4V72 | electron microscopy | 13.00 | AE | 10-159 | [»] | |
4V73 | electron microscopy | 15.00 | AE | 10-159 | [»] | |
4V74 | electron microscopy | 17.00 | AE | 10-159 | [»] | |
4V75 | electron microscopy | 12.00 | AE | 10-159 | [»] | |
4V76 | electron microscopy | 17.00 | AE | 10-159 | [»] | |
4V77 | electron microscopy | 17.00 | AE | 10-159 | [»] | |
4V78 | electron microscopy | 20.00 | AE | 10-159 | [»] | |
4V79 | electron microscopy | 15.00 | AE | 10-159 | [»] | |
4V7A | electron microscopy | 9.00 | AE | 10-159 | [»] | |
4V7B | electron microscopy | 6.80 | AE | 1-167 | [»] | |
4V7C | electron microscopy | 7.60 | AE | 2-167 | [»] | |
4V7D | electron microscopy | 7.60 | BE | 2-167 | [»] | |
4V7I | electron microscopy | 9.60 | BE | 1-167 | [»] | |
4V7S | X-ray | 3.25 | AE/CE | 10-159 | [»] | |
4V7T | X-ray | 3.19 | AE/CE | 10-159 | [»] | |
4V7U | X-ray | 3.10 | AE/CE | 10-159 | [»] | |
4V7V | X-ray | 3.29 | AE/CE | 10-159 | [»] | |
4V85 | X-ray | 3.20 | AE | 1-167 | [»] | |
4V89 | X-ray | 3.70 | AE | 1-167 | [»] | |
4V9C | X-ray | 3.30 | AE/CE | 1-167 | [»] | |
4V9D | X-ray | 3.00 | AE/BE | 10-159 | [»] | |
4V9O | X-ray | 2.90 | BE/DE/FE/HE | 1-167 | [»] | |
4V9P | X-ray | 2.90 | BE/DE/FE/HE | 1-167 | [»] | |
4WF1 | X-ray | 3.09 | AE/CE | 10-159 | [»] | |
4WOI | X-ray | 3.00 | AE/DE | 1-167 | [»] | |
4WWW | X-ray | 3.10 | QE/XE | 10-159 | [»] | |
4YBB | X-ray | 2.10 | AE/BE | 10-164 | [»] | |
5AFI | electron microscopy | 2.90 | e | 1-167 | [»] | |
5H5U | electron microscopy | 3.00 | l | 2-167 | [»] | |
5IQR | electron microscopy | 3.00 | j | 1-167 | [»] | |
5IT8 | X-ray | 3.12 | AE/BE | 10-164 | [»] | |
5J5B | X-ray | 2.80 | AE/BE | 10-164 | [»] | |
5J7L | X-ray | 3.00 | AE/BE | 10-164 | [»] | |
5J88 | X-ray | 3.32 | AE/BE | 10-164 | [»] | |
5J8A | X-ray | 3.10 | AE/BE | 10-164 | [»] | |
5J91 | X-ray | 2.96 | AE/BE | 10-164 | [»] | |
5JC9 | X-ray | 3.03 | AE/BE | 10-164 | [»] | |
5JTE | electron microscopy | 3.60 | AE | 1-167 | [»] | |
5JU8 | electron microscopy | 3.60 | AE | 1-167 | [»] | |
5KCR | electron microscopy | 3.60 | 1e | 1-167 | [»] | |
5KCS | electron microscopy | 3.90 | 1e | 1-167 | [»] | |
5KPS | electron microscopy | 3.90 | 10 | 1-167 | [»] | |
5KPV | electron microscopy | 4.10 | 9 | 1-167 | [»] | |
5KPW | electron microscopy | 3.90 | 9 | 1-167 | [»] | |
5KPX | electron microscopy | 3.90 | 9 | 1-167 | [»] | |
5L3P | electron microscopy | 3.70 | e | 1-167 | [»] | |
5LZA | electron microscopy | 3.60 | e | 10-166 | [»] | |
5LZB | electron microscopy | 5.30 | e | 10-166 | [»] | |
5LZC | electron microscopy | 4.80 | e | 10-166 | [»] | |
5LZD | electron microscopy | 3.40 | e | 10-166 | [»] | |
5LZE | electron microscopy | 3.50 | e | 10-166 | [»] | |
5LZF | electron microscopy | 4.60 | e | 10-166 | [»] | |
5MDV | electron microscopy | 2.97 | j | 1-167 | [»] | |
5MDW | electron microscopy | 3.06 | j | 1-167 | [»] | |
5MDY | electron microscopy | 3.35 | j | 1-167 | [»] | |
5MDZ | electron microscopy | 3.10 | j | 1-167 | [»] | |
5ME0 | electron microscopy | 13.50 | E | 1-167 | [»] | |
5ME1 | electron microscopy | 13.50 | E | 1-167 | [»] | |
5MGP | electron microscopy | 3.10 | e | 10-166 | [»] | |
5MY1 | electron microscopy | 7.60 | E | 2-167 | [»] | |
5NO2 | electron microscopy | 5.16 | E | 10-164 | [»] | |
5NO3 | electron microscopy | 5.16 | E | 10-164 | [»] | |
5NO4 | electron microscopy | 5.16 | E | 10-164 | [»] | |
5NP6 | electron microscopy | 3.60 | H | 10-166 | [»] | |
5NWY | electron microscopy | 2.93 | 4 | 1-166 | [»] | |
5O2R | electron microscopy | 3.40 | e | 10-166 | [»] | |
5U4I | electron microscopy | 3.50 | e | 1-167 | [»] | |
5U4J | electron microscopy | 3.70 | e | 1-167 | [»] | |
5U9F | electron microscopy | 3.20 | E | 1-167 | [»] | |
5U9G | electron microscopy | 3.20 | E | 1-167 | [»] | |
5UYK | electron microscopy | 3.90 | E | 10-166 | [»] | |
5UYL | electron microscopy | 3.60 | E | 10-166 | [»] | |
5UYM | electron microscopy | 3.20 | E | 10-166 | [»] | |
5UYN | electron microscopy | 4.00 | E | 10-166 | [»] | |
5UYP | electron microscopy | 3.90 | E | 10-166 | [»] | |
5UYQ | electron microscopy | 3.80 | E | 10-166 | [»] | |
5UZ4 | electron microscopy | 5.80 | E | 1-167 | [»] | |
5WDT | electron microscopy | 3.00 | e | 10-166 | [»] | |
5WE4 | electron microscopy | 3.10 | e | 10-166 | [»] | |
5WE6 | electron microscopy | 3.40 | e | 10-166 | [»] | |
5WFK | electron microscopy | 3.40 | e | 10-166 | [»] | |
6BU8 | electron microscopy | 3.50 | E | 10-166 | [»] | |
6BY1 | X-ray | 3.94 | AE/BE | 10-159 | [»] | |
6C4I | electron microscopy | 3.24 | e | 1-167 | [»] | |
6DNC | electron microscopy | 3.70 | RA | 1-167 | [»] | |
6ENF | electron microscopy | 3.20 | e | 10-166 | [»] | |
6ENJ | electron microscopy | 3.70 | e | 10-166 | [»] | |
6ENU | electron microscopy | 3.10 | e | 10-166 | [»] | |
6GWT | electron microscopy | 3.80 | e | 10-166 | [»] | |
6GXM | electron microscopy | 3.80 | e | 10-166 | [»] | |
6GXN | electron microscopy | 3.90 | e | 10-166 | [»] | |
6GXO | electron microscopy | 3.90 | e | 10-166 | [»] | |
6GXP | electron microscopy | 4.40 | e | 10-166 | [»] | |
6H4N | electron microscopy | 3.00 | e | 10-166 | [»] | |
6H58 | electron microscopy | 7.90 | e/ee | 10-166 | [»] | |
6HRM | electron microscopy | 2.96 | j | 10-165 | [»] | |
6I7V | X-ray | 2.90 | AE/BE | 10-159 | [»] | |
6NQB | electron microscopy | 3.80 | E | 10-158 | [»] | |
6O9J | electron microscopy | 3.90 | e | 10-159 | [»] | |
6O9K | electron microscopy | 4.00 | e | 10-159 | [»] | |
6OFX | electron microscopy | 3.30 | J | 10-166 | [»] | |
6OG7 | electron microscopy | 3.30 | J | 10-166 | [»] | |
6ORE | electron microscopy | 2.90 | j | 10-165 | [»] | |
6ORL | electron microscopy | 3.50 | j | 10-165 | [»] | |
6OST | electron microscopy | 4.20 | j | 10-165 | [»] | |
6OT3 | electron microscopy | 3.90 | j | 10-165 | [»] | |
6OUO | electron microscopy | 3.70 | j | 10-165 | [»] | |
6Q97 | electron microscopy | 3.90 | j | 10-165 | [»] | |
6Q98 | electron microscopy | 4.30 | j | 1-167 | [»] | |
6Q9A | electron microscopy | 3.70 | j | 10-165 | [»] | |
6SZS | electron microscopy | 3.06 | e | 1-167 | [»] | |
6TBV | electron microscopy | 2.70 | S051 | 1-167 | [»] | |
6TC3 | electron microscopy | 2.70 | S051 | 1-167 | [»] | |
6VWL | electron microscopy | 3.10 | d | 1-167 | [»] | |
6VWM | electron microscopy | 3.40 | d | 1-167 | [»] | |
6VWN | electron microscopy | 3.40 | d | 1-167 | [»] | |
6W6K | electron microscopy | 3.60 | E | 1-167 | [»] | |
6W77 | electron microscopy | 3.60 | E | 1-167 | [»] | |
6W7M | electron microscopy | 3.80 | E | 1-167 | [»] | |
6W7N | electron microscopy | 3.40 | E | 1-167 | [»] | |
6W7W | electron microscopy | 3.90 | D | 1-167 | [»] | |
6WD6 | electron microscopy | 3.70 | J | 10-166 | [»] | |
6WDB | electron microscopy | 4.00 | J | 10-166 | [»] | |
6WDC | electron microscopy | 4.20 | J | 10-166 | [»] | |
6WDD | electron microscopy | 3.20 | J | 10-166 | [»] | |
6WDE | electron microscopy | 3.00 | J | 10-166 | [»] | |
6WDF | electron microscopy | 3.30 | J | 10-166 | [»] | |
6WDG | electron microscopy | 3.30 | J | 10-166 | [»] | |
6WDH | electron microscopy | 4.30 | J | 10-166 | [»] | |
6WDI | electron microscopy | 4.00 | J | 10-166 | [»] | |
6WDJ | electron microscopy | 3.70 | J | 10-166 | [»] | |
6WDK | electron microscopy | 3.60 | J | 10-166 | [»] | |
6WDL | electron microscopy | 3.70 | J | 10-166 | [»] | |
6WDM | electron microscopy | 3.60 | J | 10-166 | [»] | |
6WNV | electron microscopy | 3.50 | J | 10-166 | [»] | |
6WNW | electron microscopy | 3.20 | J | 10-166 | [»] | |
6XE0 | electron microscopy | 6.80 | D | 10-159 | [»] | |
6XZA | electron microscopy | 2.66 | E1 | 10-164 | [»] | |
6XZB | electron microscopy | 2.54 | E1 | 10-164 | [»] | |
6Y69 | electron microscopy | 2.86 | e | 10-166 | [»] | |
6ZTL | electron microscopy | 3.50 | AE | 1-167 | [»] | |
7JSS | electron microscopy | 3.70 | J | 10-166 | [»] | |
7JSW | electron microscopy | 3.80 | J | 10-166 | [»] | |
7JSZ | electron microscopy | 3.70 | J | 10-166 | [»] | |
7JT1 | electron microscopy | 3.30 | J | 10-166 | [»] | |
7JT2 | electron microscopy | 3.50 | J | 10-166 | [»] | |
7JT3 | electron microscopy | 3.70 | J | 10-166 | [»] | |
SMRi | P0A7W1 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263408, 155 interactors 852107, 3 interactors |
ComplexPortali | CPX-3802, 30S small ribosomal subunit |
DIPi | DIP-10781N |
IntActi | P0A7W1, 193 interactors |
MINTi | P0A7W1 |
STRINGi | 511145.b3303 |
PTM databases
iPTMneti | P0A7W1 |
Proteomic databases
jPOSTi | P0A7W1 |
PaxDbi | P0A7W1 |
PRIDEi | P0A7W1 |
Genome annotation databases
EnsemblBacteriai | AAC76328; AAC76328; b3303 BAE77988; BAE77988; BAE77988 |
GeneIDi | 58463228 947795 |
KEGGi | ecj:JW3265 eco:b3303 |
PATRICi | fig|1411691.4.peg.3428 |
Organism-specific databases
EchoBASEi | EB0897 |
Phylogenomic databases
eggNOGi | COG0098, Bacteria |
HOGENOMi | CLU_065898_2_2_6 |
InParanoidi | P0A7W1 |
PhylomeDBi | P0A7W1 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10904-MONOMER MetaCyc:EG10904-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P0A7W1 |
PROi | PR:P0A7W1 |
Family and domain databases
Gene3Di | 3.30.230.10, 1 hit |
HAMAPi | MF_01307_B, Ribosomal_S5_B, 1 hit |
InterProi | View 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 |
PANTHERi | PTHR13718, PTHR13718, 1 hit |
Pfami | View protein in Pfam PF00333, Ribosomal_S5, 1 hit PF03719, Ribosomal_S5_C, 1 hit |
SUPFAMi | SSF54211, SSF54211, 1 hit |
TIGRFAMsi | TIGR01021, rpsE_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00585, RIBOSOMAL_S5, 1 hit PS50881, S5_DSRBD, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RS5_ECOLI | |
Accessioni | P0A7W1Primary (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: | April 7, 2021 | |
This is version 162 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Ribosomal proteins
Ribosomal proteins families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families