UniProtKB - P0A7V8 (RS4_ECOLI)
30S ribosomal protein S4
rpsD
Functioni
One of two assembly initiator proteins for the 30S subunit, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
1 PublicationWith S5 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).
Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp.
1 PublicationProtein S4 is also a translational repressor protein, it controls the translation of the alpha-operon (which codes for S13, S11, S4, RNA polymerase alpha subunit, and L17) by binding to its mRNA.
1 PublicationAlso functions as a rho-dependent antiterminator of rRNA transcription, increasing the synthesis of rRNA under conditions of excess protein, allowing a more rapid return to homeostasis. Binds directly to RNA polymerase.
1 PublicationPart of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis. This subunit may play a particular role in long-distance rRNA annealing needed for pre-rRNA processing.
1 PublicationGO - Molecular functioni
- mRNA 5'-UTR binding Source: EcoCyc
- rRNA binding Source: EcoliWiki
- structural constituent of ribosome Source: CAFA
- translation repressor activity, mRNA regulatory element binding Source: EcoCyc
GO - Biological processi
- DNA-templated transcription, termination Source: UniProtKB-KW
- maintenance of translational fidelity Source: EcoCyc
- negative regulation of translational initiation Source: EcoCyc
- positive regulation of translational fidelity Source: GO_Central
- response to antibiotic Source: UniProtKB-KW
- ribosomal small subunit assembly Source: CAFA
- transcription antitermination Source: EcoCyc
Keywordsi
Molecular function | Repressor, Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding |
Biological process | Antibiotic resistance, Ribosome biogenesis, Transcription, Transcription antitermination, Transcription regulation, Transcription termination, Translation regulation |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10903-MONOMER |
Protein family/group databases
MoonProti | P0A7V8 |
Names & Taxonomyi
Protein namesi | Recommended name: 30S ribosomal protein S4Alternative name(s): Small ribosomal subunit protein uS41 Publication |
Gene namesi | Name:rpsD Synonyms:ramA Ordered Locus Names:b3296, JW3258 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytosol
- cytosol Source: EcoCyc
- cytosolic small ribosomal subunit Source: CAFA
Other locations
- cytoplasm Source: ComplexPortal
- small ribosomal subunit Source: GO_Central
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 44 – 47 | RKPR → AKPA: Decreases mRNA unwinding ability of the ribosome. 1 Publication | 4 |
Chemistry databases
DrugBanki | DB00453, Clomocycline DB12329, Eravacycline DB00256, Lymecycline DB01017, Minocycline DB00595, Oxytetracycline |
DrugCentrali | P0A7V8 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000132380 | 2 – 206 | 30S ribosomal protein S4Add BLAST | 205 |
Proteomic databases
jPOSTi | P0A7V8 |
PaxDbi | P0A7V8 |
PRIDEi | P0A7V8 |
Interactioni
Subunit structurei
Part of the 30S ribosomal subunit (PubMed:4587210, PubMed:1100394, PubMed:7556101, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:10094780, PubMed:12244297, PubMed:27906160, PubMed:27906161, PubMed:28077875). Contacts protein S5. With proteins S3 and S5 encircles the mRNA as it enters the ribosome, which may play a role in mRNA helicase processivity (PubMed:15652481). Some nascent polypeptide chains are able to cross-link to this protein in situ (PubMed:9716382). The rRNA transcription and antitermination complex (rrnTAC) consists of RNAP, NusA, NusB, NusE (rpsJ), NusG, SubB, ribosomal protein S4, DNA and precursor rRNA; S4 is more flexible than other subunits (PubMed:32871103).
14 PublicationsBinary interactionsi
P0A7V8
With | #Exp. | IntAct |
---|---|---|
rng [P0A9J0] | 2 | EBI-543939,EBI-545964 |
Protein-protein interaction databases
BioGRIDi | 852105, 3 interactors |
ComplexPortali | CPX-3802, 30S small ribosomal subunit |
DIPi | DIP-35794N |
IntActi | P0A7V8, 233 interactors |
MINTi | P0A7V8 |
STRINGi | 511145.b3296 |
Structurei
Secondary structure
3D structure databases
SMRi | P0A7V8 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A7V8 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 96 – 156 | S4 RNA-bindingAdd BLAST | 61 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0522, Bacteria |
HOGENOMi | CLU_092403_0_2_6 |
InParanoidi | P0A7V8 |
PhylomeDBi | P0A7V8 |
Family and domain databases
CDDi | cd00165, S4, 1 hit |
Gene3Di | 3.10.290.10, 1 hit |
HAMAPi | MF_01306_B, Ribosomal_S4_B, 1 hit |
InterProi | View protein in InterPro IPR022801, Ribosomal_S4/S9 IPR001912, Ribosomal_S4/S9_N IPR005709, Ribosomal_S4_bac-type IPR018079, Ribosomal_S4_CS IPR002942, S4_RNA-bd IPR036986, S4_RNA-bd_sf |
PANTHERi | PTHR11831, PTHR11831, 1 hit PTHR11831:SF4, PTHR11831:SF4, 1 hit |
Pfami | View protein in Pfam PF00163, Ribosomal_S4, 1 hit PF01479, S4, 1 hit |
SMARTi | View protein in SMART SM01390, Ribosomal_S4, 1 hit SM00363, S4, 1 hit |
TIGRFAMsi | TIGR01017, rpsD_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00632, RIBOSOMAL_S4, 1 hit PS50889, S4, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MARYLGPKLK LSRREGTDLF LKSGVRAIDT KCKIEQAPGQ HGARKPRLSD
60 70 80 90 100
YGVQLREKQK VRRIYGVLER QFRNYYKEAA RLKGNTGENL LALLEGRLDN
110 120 130 140 150
VVYRMGFGAT RAEARQLVSH KAIMVNGRVV NIASYQVSPN DVVSIREKAK
160 170 180 190 200
KQSRVKAALE LAEQREKPTW LEVDAGKMEG TFKRKPERSD LSADINEHLI
VELYSK
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 91 | Missing AA sequence (PubMed:4587210).Curated | 1 | |
Sequence conflicti | 91 | Missing AA sequence (PubMed:1100394).Curated | 1 | |
Sequence conflicti | 95 | E → Q AA sequence (PubMed:4587210).Curated | 1 | |
Sequence conflicti | 95 | E → Q AA sequence (PubMed:1100394).Curated | 1 | |
Sequence conflicti | 138 – 144 | SPNDVVS → DPNSVV AA sequence (PubMed:4587210).Curated | 7 | |
Sequence conflicti | 138 – 144 | SPNDVVS → DPNSVV AA sequence (PubMed:1100394).Curated | 7 | |
Sequence conflicti | 152 | Q → E AA sequence (PubMed:4587210).Curated | 1 | |
Sequence conflicti | 152 | Q → E AA sequence (PubMed:1100394).Curated | 1 | |
Sequence conflicti | 166 | E → Q AA sequence (PubMed:4587210).Curated | 1 | |
Sequence conflicti | 166 | E → Q AA sequence (PubMed:1100394).Curated | 1 |
Mass spectrometryi
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 51 | Y → D in rpsD101; suppresses a temperature-sensitive mutant of release factor 1, R137P. Not a ram mutation. 1 Publication | 1 | |
Natural varianti | 170 – 206 | Missing in rpsD16; suppresses streptomycin dependence in protein S12. A ram mutation. 1 PublicationAdd BLAST | 37 | |
Natural varianti | 177 – 206 | KMEGT…ELYSK → GRYV in rpsD12; suppresses streptomycin dependence in protein S12. A ram mutation. 1 PublicationAdd BLAST | 30 | |
Natural varianti | 179 – 206 | EGTFK…ELYSK → ARYV in rpsD14; suppresses streptomycin dependence in protein S12. A ram mutation. 1 PublicationAdd BLAST | 28 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X02543 Genomic DNA Translation: CAA26394.1 U18997 Genomic DNA Translation: AAA58094.1 U00096 Genomic DNA Translation: AAC76321.1 AP009048 Genomic DNA Translation: BAE77995.1 V00353 Genomic DNA Translation: CAA23645.1 J01685 Genomic DNA Translation: AAA24576.1 |
PIRi | C23807, R3EC4 |
RefSeqi | NP_417755.1, NC_000913.3 WP_000135224.1, NZ_STEB01000038.1 |
Genome annotation databases
EnsemblBacteriai | AAC76321; AAC76321; b3296 BAE77995; BAE77995; BAE77995 |
GeneIDi | 67415337 947793 |
KEGGi | ecj:JW3258 eco:b3296 |
PATRICi | fig|1411691.4.peg.3435 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X02543 Genomic DNA Translation: CAA26394.1 U18997 Genomic DNA Translation: AAA58094.1 U00096 Genomic DNA Translation: AAC76321.1 AP009048 Genomic DNA Translation: BAE77995.1 V00353 Genomic DNA Translation: CAA23645.1 J01685 Genomic DNA Translation: AAA24576.1 |
PIRi | C23807, R3EC4 |
RefSeqi | NP_417755.1, NC_000913.3 WP_000135224.1, 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 | A | 43-200 | [»] | |
2YKR | electron microscopy | 9.80 | D | 2-206 | [»] | |
3J9Y | electron microscopy | 3.90 | d | 1-206 | [»] | |
3J9Z | electron microscopy | 3.60 | SD | 2-206 | [»] | |
3JA1 | electron microscopy | 3.60 | SD | 2-206 | [»] | |
3JBU | electron microscopy | 3.64 | D | 1-206 | [»] | |
3JBV | electron microscopy | 3.32 | D | 1-206 | [»] | |
3JCD | electron microscopy | 3.70 | d | 1-206 | [»] | |
3JCE | electron microscopy | 3.20 | d | 1-206 | [»] | |
3JCJ | electron microscopy | 3.70 | l | 1-206 | [»] | |
3JCN | electron microscopy | 4.60 | g | 1-206 | [»] | |
4A2I | electron microscopy | 16.50 | D | 2-206 | [»] | |
4ADV | electron microscopy | 13.50 | D | 2-206 | [»] | |
4U1U | X-ray | 2.95 | AD/CD | 2-206 | [»] | |
4U1V | X-ray | 3.00 | AD/CD | 2-206 | [»] | |
4U20 | X-ray | 2.90 | AD/CD | 2-206 | [»] | |
4U24 | X-ray | 2.90 | AD/CD | 2-206 | [»] | |
4U25 | X-ray | 2.90 | AD/CD | 2-206 | [»] | |
4U26 | X-ray | 2.80 | AD/CD | 2-206 | [»] | |
4U27 | X-ray | 2.80 | AD/CD | 2-206 | [»] | |
4V47 | electron microscopy | 12.30 | BD | 2-206 | [»] | |
4V48 | electron microscopy | 11.50 | BD | 2-206 | [»] | |
4V4H | X-ray | 3.46 | AD/CD | 1-206 | [»] | |
4V4Q | X-ray | 3.46 | AD/CD | 2-206 | [»] | |
4V4V | electron microscopy | 15.00 | AD | 3-206 | [»] | |
4V4W | electron microscopy | 15.00 | AD | 3-206 | [»] | |
4V50 | X-ray | 3.22 | AD/CD | 2-206 | [»] | |
4V52 | X-ray | 3.21 | AD/CD | 2-206 | [»] | |
4V53 | X-ray | 3.54 | AD/CD | 2-206 | [»] | |
4V54 | X-ray | 3.30 | AD/CD | 2-206 | [»] | |
4V55 | X-ray | 4.00 | AD/CD | 2-206 | [»] | |
4V56 | X-ray | 3.93 | AD/CD | 2-206 | [»] | |
4V57 | X-ray | 3.50 | AD/CD | 2-206 | [»] | |
4V5B | X-ray | 3.74 | BD/DD | 2-206 | [»] | |
4V5H | electron microscopy | 5.80 | AD | 2-206 | [»] | |
4V5Y | X-ray | 4.45 | AD/CD | 2-206 | [»] | |
4V64 | X-ray | 3.50 | AD/CD | 2-206 | [»] | |
4V65 | electron microscopy | 9.00 | AR | 1-206 | [»] | |
4V66 | electron microscopy | 9.00 | AR | 1-206 | [»] | |
4V69 | electron microscopy | 6.70 | AD | 2-206 | [»] | |
4V6C | X-ray | 3.19 | AD/CD | 1-206 | [»] | |
4V6D | X-ray | 3.81 | AD/CD | 1-206 | [»] | |
4V6E | X-ray | 3.71 | AD/CD | 1-206 | [»] | |
4V6K | electron microscopy | 8.25 | BH | 1-206 | [»] | |
4V6L | electron microscopy | 13.20 | AH | 1-206 | [»] | |
4V6M | electron microscopy | 7.10 | AD | 2-206 | [»] | |
4V6N | electron microscopy | 12.10 | BG | 2-206 | [»] | |
4V6O | electron microscopy | 14.70 | AG | 2-206 | [»] | |
4V6P | electron microscopy | 13.50 | AG | 2-206 | [»] | |
4V6Q | electron microscopy | 11.50 | AG | 2-206 | [»] | |
4V6R | electron microscopy | 11.50 | AG | 2-206 | [»] | |
4V6S | electron microscopy | 13.10 | BF | 2-206 | [»] | |
4V6T | electron microscopy | 8.30 | AD | 2-206 | [»] | |
4V6V | electron microscopy | 9.80 | AD | 2-206 | [»] | |
4V6Y | electron microscopy | 12.00 | AD | 1-206 | [»] | |
4V6Z | electron microscopy | 12.00 | AD | 1-206 | [»] | |
4V70 | electron microscopy | 17.00 | AD | 1-206 | [»] | |
4V71 | electron microscopy | 20.00 | AD | 1-206 | [»] | |
4V72 | electron microscopy | 13.00 | AD | 1-206 | [»] | |
4V73 | electron microscopy | 15.00 | AD | 1-206 | [»] | |
4V74 | electron microscopy | 17.00 | AD | 1-206 | [»] | |
4V75 | electron microscopy | 12.00 | AD | 1-206 | [»] | |
4V76 | electron microscopy | 17.00 | AD | 1-206 | [»] | |
4V77 | electron microscopy | 17.00 | AD | 1-206 | [»] | |
4V78 | electron microscopy | 20.00 | AD | 1-206 | [»] | |
4V79 | electron microscopy | 15.00 | AD | 1-206 | [»] | |
4V7A | electron microscopy | 9.00 | AD | 1-206 | [»] | |
4V7B | electron microscopy | 6.80 | AD | 1-206 | [»] | |
4V7C | electron microscopy | 7.60 | AD | 2-206 | [»] | |
4V7D | electron microscopy | 7.60 | BD | 2-206 | [»] | |
4V7I | electron microscopy | 9.60 | BD | 1-206 | [»] | |
4V7S | X-ray | 3.25 | AD/CD | 2-206 | [»] | |
4V7T | X-ray | 3.19 | AD/CD | 2-206 | [»] | |
4V7U | X-ray | 3.10 | AD/CD | 2-206 | [»] | |
4V7V | X-ray | 3.29 | AD/CD | 2-206 | [»] | |
4V85 | X-ray | 3.20 | AD | 1-206 | [»] | |
4V89 | X-ray | 3.70 | AD | 1-206 | [»] | |
4V9C | X-ray | 3.30 | AD/CD | 1-206 | [»] | |
4V9D | X-ray | 3.00 | AD/BD | 2-206 | [»] | |
4V9O | X-ray | 2.90 | BD/DD/FD/HD | 1-206 | [»] | |
4V9P | X-ray | 2.90 | BD/DD/FD/HD | 1-206 | [»] | |
4WF1 | X-ray | 3.09 | AD/CD | 2-206 | [»] | |
4WOI | X-ray | 3.00 | AD/DD | 1-206 | [»] | |
4WWW | X-ray | 3.10 | QD/XD | 2-206 | [»] | |
4YBB | X-ray | 2.10 | AD/BD | 2-206 | [»] | |
5AFI | electron microscopy | 2.90 | d | 1-206 | [»] | |
5H5U | electron microscopy | 3.00 | k | 2-206 | [»] | |
5IQR | electron microscopy | 3.00 | i | 1-206 | [»] | |
5IT8 | X-ray | 3.12 | AD/BD | 2-206 | [»] | |
5J5B | X-ray | 2.80 | AD/BD | 2-206 | [»] | |
5J7L | X-ray | 3.00 | AD/BD | 2-206 | [»] | |
5J88 | X-ray | 3.32 | AD/BD | 2-206 | [»] | |
5J8A | X-ray | 3.10 | AD/BD | 2-206 | [»] | |
5J91 | X-ray | 2.96 | AD/BD | 2-206 | [»] | |
5JC9 | X-ray | 3.03 | AD/BD | 2-206 | [»] | |
5JTE | electron microscopy | 3.60 | AD | 1-206 | [»] | |
5JU8 | electron microscopy | 3.60 | AD | 1-206 | [»] | |
5KCR | electron microscopy | 3.60 | 1d | 1-206 | [»] | |
5KCS | electron microscopy | 3.90 | 1d | 1-206 | [»] | |
5KPS | electron microscopy | 3.90 | 9 | 1-206 | [»] | |
5KPV | electron microscopy | 4.10 | 8 | 1-206 | [»] | |
5KPW | electron microscopy | 3.90 | 8 | 1-206 | [»] | |
5KPX | electron microscopy | 3.90 | 8 | 1-206 | [»] | |
5L3P | electron microscopy | 3.70 | d | 1-206 | [»] | |
5LZA | electron microscopy | 3.60 | d | 2-206 | [»] | |
5LZB | electron microscopy | 5.30 | d | 2-206 | [»] | |
5LZC | electron microscopy | 4.80 | d | 2-206 | [»] | |
5LZD | electron microscopy | 3.40 | d | 2-206 | [»] | |
5LZE | electron microscopy | 3.50 | d | 2-206 | [»] | |
5LZF | electron microscopy | 4.60 | d | 2-206 | [»] | |
5MDV | electron microscopy | 2.97 | i | 1-206 | [»] | |
5MDW | electron microscopy | 3.06 | i | 1-206 | [»] | |
5MDY | electron microscopy | 3.35 | i | 1-206 | [»] | |
5MDZ | electron microscopy | 3.10 | i | 1-206 | [»] | |
5ME0 | electron microscopy | 13.50 | D | 1-206 | [»] | |
5ME1 | electron microscopy | 13.50 | D | 1-206 | [»] | |
5MGP | electron microscopy | 3.10 | d | 2-206 | [»] | |
5MY1 | electron microscopy | 7.60 | D | 2-206 | [»] | |
5NO2 | electron microscopy | 5.16 | D | 2-206 | [»] | |
5NO3 | electron microscopy | 5.16 | D | 2-206 | [»] | |
5NO4 | electron microscopy | 5.16 | D | 2-206 | [»] | |
5NP6 | electron microscopy | 3.60 | G | 2-206 | [»] | |
5NWY | electron microscopy | 2.93 | 3 | 1-206 | [»] | |
5O2R | electron microscopy | 3.40 | d | 2-206 | [»] | |
5U4I | electron microscopy | 3.50 | d | 1-206 | [»] | |
5U4J | electron microscopy | 3.70 | d | 1-206 | [»] | |
5U9F | electron microscopy | 3.20 | D | 1-206 | [»] | |
5U9G | electron microscopy | 3.20 | D | 1-206 | [»] | |
5UYK | electron microscopy | 3.90 | D | 2-206 | [»] | |
5UYL | electron microscopy | 3.60 | D | 2-206 | [»] | |
5UYM | electron microscopy | 3.20 | D | 2-206 | [»] | |
5UYN | electron microscopy | 4.00 | D | 2-206 | [»] | |
5UYP | electron microscopy | 3.90 | D | 2-206 | [»] | |
5UYQ | electron microscopy | 3.80 | D | 2-206 | [»] | |
5UZ4 | electron microscopy | 5.80 | D | 1-206 | [»] | |
5WDT | electron microscopy | 3.00 | d | 2-206 | [»] | |
5WE4 | electron microscopy | 3.10 | d | 2-206 | [»] | |
5WE6 | electron microscopy | 3.40 | d | 2-206 | [»] | |
5WFK | electron microscopy | 3.40 | d | 2-206 | [»] | |
6BU8 | electron microscopy | 3.50 | D | 2-206 | [»] | |
6BY1 | X-ray | 3.94 | AD/BD | 2-206 | [»] | |
6C4I | electron microscopy | 3.24 | d | 1-206 | [»] | |
6ENF | electron microscopy | 3.20 | d | 2-206 | [»] | |
6ENJ | electron microscopy | 3.70 | d | 2-206 | [»] | |
6ENU | electron microscopy | 3.10 | d | 2-206 | [»] | |
6GWT | electron microscopy | 3.80 | d | 2-206 | [»] | |
6GXM | electron microscopy | 3.80 | d | 2-206 | [»] | |
6GXN | electron microscopy | 3.90 | d | 2-206 | [»] | |
6GXO | electron microscopy | 3.90 | d | 2-206 | [»] | |
6GXP | electron microscopy | 4.40 | d | 2-206 | [»] | |
6H4N | electron microscopy | 3.00 | d | 2-206 | [»] | |
6H58 | electron microscopy | 7.90 | d/dd | 2-206 | [»] | |
6HRM | electron microscopy | 2.96 | i | 2-206 | [»] | |
6I7V | X-ray | 2.90 | AD/BD | 2-206 | [»] | |
6NQB | electron microscopy | 3.80 | D | 2-206 | [»] | |
6O9J | electron microscopy | 3.90 | d | 2-206 | [»] | |
6O9K | electron microscopy | 4.00 | d | 2-206 | [»] | |
6OFX | electron microscopy | 3.30 | I | 2-206 | [»] | |
6OG7 | electron microscopy | 3.30 | I | 2-206 | [»] | |
6ORE | electron microscopy | 2.90 | i | 2-206 | [»] | |
6ORL | electron microscopy | 3.50 | i | 2-206 | [»] | |
6OST | electron microscopy | 4.20 | i | 2-206 | [»] | |
6OT3 | electron microscopy | 3.90 | i | 2-206 | [»] | |
6OUO | electron microscopy | 3.70 | i | 2-206 | [»] | |
6Q97 | electron microscopy | 3.90 | i | 2-206 | [»] | |
6Q98 | electron microscopy | 4.30 | i | 1-206 | [»] | |
6Q9A | electron microscopy | 3.70 | i | 2-206 | [»] | |
6SZS | electron microscopy | 3.06 | d | 1-206 | [»] | |
6TBV | electron microscopy | 2.70 | S041 | 1-206 | [»] | |
6TC3 | electron microscopy | 2.70 | S041 | 1-206 | [»] | |
6TQO | electron microscopy | 4.00 | C | 1-206 | [»] | |
6VWL | electron microscopy | 3.10 | c | 1-206 | [»] | |
6VWM | electron microscopy | 3.40 | c | 1-206 | [»] | |
6VWN | electron microscopy | 3.40 | c | 1-206 | [»] | |
6W6K | electron microscopy | 3.60 | D | 1-206 | [»] | |
6W77 | electron microscopy | 3.60 | D | 1-206 | [»] | |
6W7M | electron microscopy | 3.80 | D | 1-206 | [»] | |
6W7N | electron microscopy | 3.40 | D | 1-206 | [»] | |
6W7W | electron microscopy | 3.90 | C | 1-206 | [»] | |
6WD6 | electron microscopy | 3.70 | I | 2-206 | [»] | |
6WDB | electron microscopy | 4.00 | I | 2-206 | [»] | |
6WDC | electron microscopy | 4.20 | I | 2-206 | [»] | |
6WDD | electron microscopy | 3.20 | I | 2-206 | [»] | |
6WDE | electron microscopy | 3.00 | I | 2-206 | [»] | |
6WDF | electron microscopy | 3.30 | I | 2-206 | [»] | |
6WDG | electron microscopy | 3.30 | I | 2-206 | [»] | |
6WDH | electron microscopy | 4.30 | I | 2-206 | [»] | |
6WDI | electron microscopy | 4.00 | I | 2-206 | [»] | |
6WDJ | electron microscopy | 3.70 | I | 2-206 | [»] | |
6WDK | electron microscopy | 3.60 | I | 2-206 | [»] | |
6WDL | electron microscopy | 3.70 | I | 2-206 | [»] | |
6WDM | electron microscopy | 3.60 | I | 2-206 | [»] | |
6WNV | electron microscopy | 3.50 | I | 2-206 | [»] | |
6WNW | electron microscopy | 3.20 | I | 2-206 | [»] | |
6XE0 | electron microscopy | 6.80 | C | 2-206 | [»] | |
6XZA | electron microscopy | 2.66 | D1 | 2-206 | [»] | |
6XZB | electron microscopy | 2.54 | D1 | 2-206 | [»] | |
6Y69 | electron microscopy | 2.86 | d | 2-206 | [»] | |
6ZTL | electron microscopy | 3.50 | AD | 1-206 | [»] | |
7ABZ | electron microscopy | 3.21 | i | 2-206 | [»] | |
7AC7 | electron microscopy | 3.08 | i | 2-206 | [»] | |
7ACJ | electron microscopy | 3.20 | i | 2-206 | [»] | |
7ACR | electron microscopy | 3.44 | i | 2-206 | [»] | |
7B5K | electron microscopy | 2.90 | d | 2-206 | [»] | |
7BOD | electron microscopy | 2.88 | D | 1-206 | [»] | |
7BOF | electron microscopy | 2.92 | D | 1-206 | [»] | |
7BOG | electron microscopy | 2.75 | D | 1-206 | [»] | |
7BOI | electron microscopy | 2.98 | D | 1-206 | [»] | |
7D6Z | electron microscopy | 3.40 | k | 1-206 | [»] | |
7D80 | electron microscopy | 4.10 | E | 1-206 | [»] | |
7JSS | electron microscopy | 3.70 | I | 2-206 | [»] | |
7JSW | electron microscopy | 3.80 | I | 2-206 | [»] | |
7JSZ | electron microscopy | 3.70 | I | 2-206 | [»] | |
7JT1 | electron microscopy | 3.30 | I | 2-206 | [»] | |
7JT2 | electron microscopy | 3.50 | I | 2-206 | [»] | |
7JT3 | electron microscopy | 3.70 | I | 2-206 | [»] | |
7K50 | electron microscopy | 3.40 | I | 2-206 | [»] | |
7K51 | electron microscopy | 3.50 | I | 2-206 | [»] | |
7K52 | electron microscopy | 3.40 | I | 2-206 | [»] | |
7K53 | electron microscopy | 3.20 | I | 2-206 | [»] | |
7K54 | electron microscopy | 3.20 | I | 2-206 | [»] | |
7K55 | electron microscopy | 3.30 | I | 2-206 | [»] | |
7LV0 | electron microscopy | 3.20 | I | 2-206 | [»] | |
7N1P | electron microscopy | 2.33 | SD | 1-206 | [»] | |
7N2C | electron microscopy | 2.72 | SD | 1-206 | [»] | |
7N2U | electron microscopy | 2.53 | SD | 1-206 | [»] | |
7N2V | electron microscopy | 2.54 | SD | 1-206 | [»] | |
7N30 | electron microscopy | 2.66 | SD | 1-206 | [»] | |
7N31 | electron microscopy | 2.69 | SD | 1-206 | [»] | |
7NAS | electron microscopy | 3.31 | D | 1-206 | [»] | |
7O19 | electron microscopy | 2.90 | AD | 1-206 | [»] | |
7O1A | electron microscopy | 2.40 | AD | 1-206 | [»] | |
7O1C | electron microscopy | 2.60 | AD | 1-206 | [»] | |
7O5H | electron microscopy | 3.10 | D | 2-206 | [»] | |
7OIZ | electron microscopy | 2.90 | D | 1-206 | [»] | |
7OJ0 | electron microscopy | 3.50 | D | 1-206 | [»] | |
7P3K | electron microscopy | 2.90 | D | 1-206 | [»] | |
7PJV | electron microscopy | 3.10 | d | 1-206 | [»] | |
7PJY | electron microscopy | 3.10 | d | 1-206 | [»] | |
SMRi | P0A7V8 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 852105, 3 interactors |
ComplexPortali | CPX-3802, 30S small ribosomal subunit |
DIPi | DIP-35794N |
IntActi | P0A7V8, 233 interactors |
MINTi | P0A7V8 |
STRINGi | 511145.b3296 |
Chemistry databases
DrugBanki | DB00453, Clomocycline DB12329, Eravacycline DB00256, Lymecycline DB01017, Minocycline DB00595, Oxytetracycline |
DrugCentrali | P0A7V8 |
Protein family/group databases
MoonProti | P0A7V8 |
Proteomic databases
jPOSTi | P0A7V8 |
PaxDbi | P0A7V8 |
PRIDEi | P0A7V8 |
Genome annotation databases
EnsemblBacteriai | AAC76321; AAC76321; b3296 BAE77995; BAE77995; BAE77995 |
GeneIDi | 67415337 947793 |
KEGGi | ecj:JW3258 eco:b3296 |
PATRICi | fig|1411691.4.peg.3435 |
Organism-specific databases
EchoBASEi | EB0896 |
Phylogenomic databases
eggNOGi | COG0522, Bacteria |
HOGENOMi | CLU_092403_0_2_6 |
InParanoidi | P0A7V8 |
PhylomeDBi | P0A7V8 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10903-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P0A7V8 |
PROi | PR:P0A7V8 |
Family and domain databases
CDDi | cd00165, S4, 1 hit |
Gene3Di | 3.10.290.10, 1 hit |
HAMAPi | MF_01306_B, Ribosomal_S4_B, 1 hit |
InterProi | View protein in InterPro IPR022801, Ribosomal_S4/S9 IPR001912, Ribosomal_S4/S9_N IPR005709, Ribosomal_S4_bac-type IPR018079, Ribosomal_S4_CS IPR002942, S4_RNA-bd IPR036986, S4_RNA-bd_sf |
PANTHERi | PTHR11831, PTHR11831, 1 hit PTHR11831:SF4, PTHR11831:SF4, 1 hit |
Pfami | View protein in Pfam PF00163, Ribosomal_S4, 1 hit PF01479, S4, 1 hit |
SMARTi | View protein in SMART SM01390, Ribosomal_S4, 1 hit SM00363, S4, 1 hit |
TIGRFAMsi | TIGR01017, rpsD_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00632, RIBOSOMAL_S4, 1 hit PS50889, S4, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | RS4_ECOLI | |
Accessioni | P0A7V8Primary (citable) accession number: P0A7V8 Secondary accession number(s): P02354, Q2M6W1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 169 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