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Protein

30S ribosomal protein S4

Gene

rpsD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.
With 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.
Protein 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.
Also 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.

GO - Molecular functioni

  • mRNA 5'-UTR binding Source: EcoCyc
  • rRNA binding Source: EcoliWiki
  • structural constituent of ribosome Source: GO_Central
  • translation repressor activity, nucleic acid 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
  • transcription antitermination Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Repressor, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Antibiotic resistance, Transcription, Transcription regulation, Transcription termination, Translation regulation

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10903-MONOMER.
ECOL316407:JW3258-MONOMER.
MetaCyc:EG10903-MONOMER.

Protein family/group databases

MoonProtiP0A7V8.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S4
Gene namesi
Name:rpsD
Synonyms:ramA
Ordered Locus Names:b3296, JW3258
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10903. rpsD.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi44 – 47RKPR → AKPA: Decreases mRNA unwinding ability of the ribosome. 1 Publication4

Chemistry databases

DrugBankiDB00453. Clomocycline.
DB00618. Demeclocycline.
DB00254. Doxycycline.
DB00256. Lymecycline.
DB01017. Minocycline.
DB00595. Oxytetracycline.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001323802 – 20630S ribosomal protein S4Add BLAST205

Proteomic databases

EPDiP0A7V8.
PaxDbiP0A7V8.
PRIDEiP0A7V8.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. 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. Some nascent polypeptide chains are able to cross-link to this protein in situ.

Protein-protein interaction databases

BioGridi852105. 1 interactor.
DIPiDIP-35794N.
IntActiP0A7V8. 214 interactors.
MINTiMINT-6478162.
STRINGi511145.b3296.

Structurei

Secondary structure

1206
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 15Combined sources7
Beta strandi20 – 22Combined sources3
Beta strandi24 – 26Combined sources3
Beta strandi28 – 32Combined sources5
Beta strandi34 – 36Combined sources3
Beta strandi38 – 41Combined sources4
Beta strandi42 – 44Combined sources3
Helixi50 – 65Combined sources16
Helixi69 – 81Combined sources13
Beta strandi82 – 84Combined sources3
Helixi86 – 95Combined sources10
Helixi98 – 104Combined sources7
Beta strandi107 – 110Combined sources4
Helixi111 – 119Combined sources9
Turni120 – 122Combined sources3
Beta strandi124 – 129Combined sources6
Beta strandi132 – 134Combined sources3
Beta strandi142 – 144Combined sources3
Turni147 – 151Combined sources5
Helixi153 – 164Combined sources12
Beta strandi169 – 172Combined sources4
Beta strandi175 – 177Combined sources3
Beta strandi179 – 182Combined sources4
Helixi188 – 190Combined sources3
Beta strandi193 – 195Combined sources3
Helixi197 – 203Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50A43-200[»]
1M5Gmodel-D2-206[»]
2YKRelectron microscopy9.80D2-206[»]
3J9Yelectron microscopy3.90d1-206[»]
3J9Zelectron microscopy3.60SD2-206[»]
3JA1electron microscopy3.60SD2-206[»]
3JBUelectron microscopy3.64D1-206[»]
3JBVelectron microscopy3.32D1-206[»]
3JCDelectron microscopy3.70d1-206[»]
3JCEelectron microscopy3.20d1-206[»]
3JCJelectron microscopy3.70l1-206[»]
3JCNelectron microscopy4.60g1-206[»]
4A2Ielectron microscopy16.50D2-206[»]
4ADVelectron microscopy13.50D2-206[»]
4U1UX-ray2.95AD/CD2-206[»]
4U1VX-ray3.00AD/CD2-206[»]
4U20X-ray2.90AD/CD2-206[»]
4U24X-ray2.90AD/CD2-206[»]
4U25X-ray2.90AD/CD2-206[»]
4U26X-ray2.80AD/CD2-206[»]
4U27X-ray2.80AD/CD2-206[»]
4V47electron microscopy12.30BD2-206[»]
4V48electron microscopy11.50BD2-206[»]
4V4HX-ray3.46AD/CD1-206[»]
4V4QX-ray3.46AD/CD2-206[»]
4V4Velectron microscopy15.00AD3-206[»]
4V4Welectron microscopy15.00AD3-206[»]
4V50X-ray3.22AD/CD2-206[»]
4V52X-ray3.21AD/CD2-206[»]
4V53X-ray3.54AD/CD2-206[»]
4V54X-ray3.30AD/CD2-206[»]
4V55X-ray4.00AD/CD2-206[»]
4V56X-ray3.93AD/CD2-206[»]
4V57X-ray3.50AD/CD2-206[»]
4V5BX-ray3.74BD/DD2-206[»]
4V5Helectron microscopy5.80AD2-206[»]
4V5YX-ray4.45AD/CD2-206[»]
4V64X-ray3.50AD/CD2-206[»]
4V65electron microscopy9.00AR1-206[»]
4V66electron microscopy9.00AR1-206[»]
4V69electron microscopy6.70AD2-206[»]
4V6CX-ray3.19AD/CD1-206[»]
4V6DX-ray3.81AD/CD1-206[»]
4V6EX-ray3.71AD/CD1-206[»]
4V6Kelectron microscopy8.25BH1-206[»]
4V6Lelectron microscopy13.20AH1-206[»]
4V6Melectron microscopy7.10AD2-206[»]
4V6Nelectron microscopy12.10BG2-206[»]
4V6Oelectron microscopy14.70AG2-206[»]
4V6Pelectron microscopy13.50AG2-206[»]
4V6Qelectron microscopy11.50AG2-206[»]
4V6Relectron microscopy11.50AG2-206[»]
4V6Selectron microscopy13.10BF2-206[»]
4V6Telectron microscopy8.30AD2-206[»]
4V6Velectron microscopy9.80AD2-206[»]
4V6Yelectron microscopy12.00AD1-206[»]
4V6Zelectron microscopy12.00AD1-206[»]
4V70electron microscopy17.00AD1-206[»]
4V71electron microscopy20.00AD1-206[»]
4V72electron microscopy13.00AD1-206[»]
4V73electron microscopy15.00AD1-206[»]
4V74electron microscopy17.00AD1-206[»]
4V75electron microscopy12.00AD1-206[»]
4V76electron microscopy17.00AD1-206[»]
4V77electron microscopy17.00AD1-206[»]
4V78electron microscopy20.00AD1-206[»]
4V79electron microscopy15.00AD1-206[»]
4V7Aelectron microscopy9.00AD1-206[»]
4V7Belectron microscopy6.80AD1-206[»]
4V7Celectron microscopy7.60AD2-206[»]
4V7Delectron microscopy7.60BD2-206[»]
4V7Ielectron microscopy9.60BD1-206[»]
4V7SX-ray3.25AD/CD2-206[»]
4V7TX-ray3.19AD/CD2-206[»]
4V7UX-ray3.10AD/CD2-206[»]
4V7VX-ray3.29AD/CD2-206[»]
4V85X-ray3.20AD1-206[»]
4V89X-ray3.70AD1-206[»]
4V9CX-ray3.30AD/CD1-206[»]
4V9DX-ray3.00AD/BD2-206[»]
4V9OX-ray2.90BD/DD/FD/HD1-206[»]
4V9PX-ray2.90BD/DD/FD/HD1-206[»]
4WF1X-ray3.09AD/CD2-206[»]
4WOIX-ray3.00AD/DD1-206[»]
4WWWX-ray3.10QD/XD2-206[»]
4YBBX-ray2.10AD/BD2-206[»]
5AFIelectron microscopy2.90d1-206[»]
5IQRelectron microscopy3.00i1-206[»]
5IT8X-ray3.12AD/BD2-206[»]
5J5BX-ray2.80AD/BD2-206[»]
5J7LX-ray3.00AD/BD2-206[»]
5J88X-ray3.32AD/BD2-206[»]
5J8AX-ray3.10AD/BD2-206[»]
5J91X-ray2.96AD/BD2-206[»]
5JC9X-ray3.03AD/BD2-206[»]
5JTEelectron microscopy3.60AD1-206[»]
5JU8electron microscopy3.60AD1-206[»]
5KCRelectron microscopy3.601d1-206[»]
5KCSelectron microscopy3.901d1-206[»]
5KPSelectron microscopy3.9091-206[»]
5KPVelectron microscopy4.1081-206[»]
5KPWelectron microscopy3.9081-206[»]
5KPXelectron microscopy3.9081-206[»]
5L3Pelectron microscopy3.70d1-206[»]
ProteinModelPortaliP0A7V8.
SMRiP0A7V8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7V8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini96 – 156S4 RNA-bindingAdd BLAST61

Sequence similaritiesi

Belongs to the ribosomal protein S4P family.Curated
Contains 1 S4 RNA-binding domain.Curated

Phylogenomic databases

eggNOGiENOG4105G6W. Bacteria.
COG0522. LUCA.
HOGENOMiHOG000221003.
InParanoidiP0A7V8.
KOiK02986.
OMAiRTSDYGN.
PhylomeDBiP0A7V8.

Family and domain databases

Gene3Di1.10.1050.10. 1 hit.
3.10.290.10. 1 hit.
HAMAPiMF_01306_B. Ribosomal_S4_B. 1 hit.
InterProiIPR022801. Ribosomal_S4/S9.
IPR001912. Ribosomal_S4/S9_N.
IPR005709. Ribosomal_S4_bac-type.
IPR018079. Ribosomal_S4_CS.
IPR002942. S4_RNA-bd.
[Graphical view]
PANTHERiPTHR11831. PTHR11831. 1 hit.
PfamiPF00163. Ribosomal_S4. 1 hit.
PF01479. S4. 1 hit.
[Graphical view]
SMARTiSM01390. Ribosomal_S4. 1 hit.
SM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01017. rpsD_bact. 1 hit.
PROSITEiPS00632. RIBOSOMAL_S4. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7V8-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:206
Mass (Da):23,469
Last modified:January 23, 2007 - v2
Checksum:i4015969DF8E582BB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti91Missing AA sequence (PubMed:4587210).Curated1
Sequence conflicti91Missing AA sequence (PubMed:1100394).Curated1
Sequence conflicti95E → Q AA sequence (PubMed:4587210).Curated1
Sequence conflicti95E → Q AA sequence (PubMed:1100394).Curated1
Sequence conflicti138 – 144SPNDVVS → DPNSVV AA sequence (PubMed:4587210).Curated7
Sequence conflicti138 – 144SPNDVVS → DPNSVV AA sequence (PubMed:1100394).Curated7
Sequence conflicti152Q → E AA sequence (PubMed:4587210).Curated1
Sequence conflicti152Q → E AA sequence (PubMed:1100394).Curated1
Sequence conflicti166E → Q AA sequence (PubMed:4587210).Curated1
Sequence conflicti166E → Q AA sequence (PubMed:1100394).Curated1

Mass spectrometryi

Molecular mass is 23339.5 Da from positions 2 - 206. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti51Y → D in rpsD101; suppresses a temperature-sensitive mutant of release factor 1, R137P. Not a ram mutation. 1
Natural varianti170 – 206Missing in rpsD16; suppresses streptomycin dependence in protein S12. A ram mutation. Add BLAST37
Natural varianti177 – 206KMEGT…ELYSK → GRYV in rpsD12; suppresses streptomycin dependence in protein S12. A ram mutation. Add BLAST30
Natural varianti179 – 206EGTFK…ELYSK → ARYV in rpsD14; suppresses streptomycin dependence in protein S12. A ram mutation. Add BLAST28

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.
PIRiC23807. R3EC4.
RefSeqiNP_417755.1. NC_000913.3.
WP_000135224.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76321; AAC76321; b3296.
BAE77995; BAE77995; BAE77995.
GeneIDi947793.
KEGGiecj:JW3258.
eco:b3296.
PATRICi32122024. VBIEscCol129921_3389.

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.
PIRiC23807. R3EC4.
RefSeqiNP_417755.1. NC_000913.3.
WP_000135224.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG0electron microscopy11.50A43-200[»]
1M5Gmodel-D2-206[»]
2YKRelectron microscopy9.80D2-206[»]
3J9Yelectron microscopy3.90d1-206[»]
3J9Zelectron microscopy3.60SD2-206[»]
3JA1electron microscopy3.60SD2-206[»]
3JBUelectron microscopy3.64D1-206[»]
3JBVelectron microscopy3.32D1-206[»]
3JCDelectron microscopy3.70d1-206[»]
3JCEelectron microscopy3.20d1-206[»]
3JCJelectron microscopy3.70l1-206[»]
3JCNelectron microscopy4.60g1-206[»]
4A2Ielectron microscopy16.50D2-206[»]
4ADVelectron microscopy13.50D2-206[»]
4U1UX-ray2.95AD/CD2-206[»]
4U1VX-ray3.00AD/CD2-206[»]
4U20X-ray2.90AD/CD2-206[»]
4U24X-ray2.90AD/CD2-206[»]
4U25X-ray2.90AD/CD2-206[»]
4U26X-ray2.80AD/CD2-206[»]
4U27X-ray2.80AD/CD2-206[»]
4V47electron microscopy12.30BD2-206[»]
4V48electron microscopy11.50BD2-206[»]
4V4HX-ray3.46AD/CD1-206[»]
4V4QX-ray3.46AD/CD2-206[»]
4V4Velectron microscopy15.00AD3-206[»]
4V4Welectron microscopy15.00AD3-206[»]
4V50X-ray3.22AD/CD2-206[»]
4V52X-ray3.21AD/CD2-206[»]
4V53X-ray3.54AD/CD2-206[»]
4V54X-ray3.30AD/CD2-206[»]
4V55X-ray4.00AD/CD2-206[»]
4V56X-ray3.93AD/CD2-206[»]
4V57X-ray3.50AD/CD2-206[»]
4V5BX-ray3.74BD/DD2-206[»]
4V5Helectron microscopy5.80AD2-206[»]
4V5YX-ray4.45AD/CD2-206[»]
4V64X-ray3.50AD/CD2-206[»]
4V65electron microscopy9.00AR1-206[»]
4V66electron microscopy9.00AR1-206[»]
4V69electron microscopy6.70AD2-206[»]
4V6CX-ray3.19AD/CD1-206[»]
4V6DX-ray3.81AD/CD1-206[»]
4V6EX-ray3.71AD/CD1-206[»]
4V6Kelectron microscopy8.25BH1-206[»]
4V6Lelectron microscopy13.20AH1-206[»]
4V6Melectron microscopy7.10AD2-206[»]
4V6Nelectron microscopy12.10BG2-206[»]
4V6Oelectron microscopy14.70AG2-206[»]
4V6Pelectron microscopy13.50AG2-206[»]
4V6Qelectron microscopy11.50AG2-206[»]
4V6Relectron microscopy11.50AG2-206[»]
4V6Selectron microscopy13.10BF2-206[»]
4V6Telectron microscopy8.30AD2-206[»]
4V6Velectron microscopy9.80AD2-206[»]
4V6Yelectron microscopy12.00AD1-206[»]
4V6Zelectron microscopy12.00AD1-206[»]
4V70electron microscopy17.00AD1-206[»]
4V71electron microscopy20.00AD1-206[»]
4V72electron microscopy13.00AD1-206[»]
4V73electron microscopy15.00AD1-206[»]
4V74electron microscopy17.00AD1-206[»]
4V75electron microscopy12.00AD1-206[»]
4V76electron microscopy17.00AD1-206[»]
4V77electron microscopy17.00AD1-206[»]
4V78electron microscopy20.00AD1-206[»]
4V79electron microscopy15.00AD1-206[»]
4V7Aelectron microscopy9.00AD1-206[»]
4V7Belectron microscopy6.80AD1-206[»]
4V7Celectron microscopy7.60AD2-206[»]
4V7Delectron microscopy7.60BD2-206[»]
4V7Ielectron microscopy9.60BD1-206[»]
4V7SX-ray3.25AD/CD2-206[»]
4V7TX-ray3.19AD/CD2-206[»]
4V7UX-ray3.10AD/CD2-206[»]
4V7VX-ray3.29AD/CD2-206[»]
4V85X-ray3.20AD1-206[»]
4V89X-ray3.70AD1-206[»]
4V9CX-ray3.30AD/CD1-206[»]
4V9DX-ray3.00AD/BD2-206[»]
4V9OX-ray2.90BD/DD/FD/HD1-206[»]
4V9PX-ray2.90BD/DD/FD/HD1-206[»]
4WF1X-ray3.09AD/CD2-206[»]
4WOIX-ray3.00AD/DD1-206[»]
4WWWX-ray3.10QD/XD2-206[»]
4YBBX-ray2.10AD/BD2-206[»]
5AFIelectron microscopy2.90d1-206[»]
5IQRelectron microscopy3.00i1-206[»]
5IT8X-ray3.12AD/BD2-206[»]
5J5BX-ray2.80AD/BD2-206[»]
5J7LX-ray3.00AD/BD2-206[»]
5J88X-ray3.32AD/BD2-206[»]
5J8AX-ray3.10AD/BD2-206[»]
5J91X-ray2.96AD/BD2-206[»]
5JC9X-ray3.03AD/BD2-206[»]
5JTEelectron microscopy3.60AD1-206[»]
5JU8electron microscopy3.60AD1-206[»]
5KCRelectron microscopy3.601d1-206[»]
5KCSelectron microscopy3.901d1-206[»]
5KPSelectron microscopy3.9091-206[»]
5KPVelectron microscopy4.1081-206[»]
5KPWelectron microscopy3.9081-206[»]
5KPXelectron microscopy3.9081-206[»]
5L3Pelectron microscopy3.70d1-206[»]
ProteinModelPortaliP0A7V8.
SMRiP0A7V8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852105. 1 interactor.
DIPiDIP-35794N.
IntActiP0A7V8. 214 interactors.
MINTiMINT-6478162.
STRINGi511145.b3296.

Chemistry databases

DrugBankiDB00453. Clomocycline.
DB00618. Demeclocycline.
DB00254. Doxycycline.
DB00256. Lymecycline.
DB01017. Minocycline.
DB00595. Oxytetracycline.

Protein family/group databases

MoonProtiP0A7V8.

Proteomic databases

EPDiP0A7V8.
PaxDbiP0A7V8.
PRIDEiP0A7V8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76321; AAC76321; b3296.
BAE77995; BAE77995; BAE77995.
GeneIDi947793.
KEGGiecj:JW3258.
eco:b3296.
PATRICi32122024. VBIEscCol129921_3389.

Organism-specific databases

EchoBASEiEB0896.
EcoGeneiEG10903. rpsD.

Phylogenomic databases

eggNOGiENOG4105G6W. Bacteria.
COG0522. LUCA.
HOGENOMiHOG000221003.
InParanoidiP0A7V8.
KOiK02986.
OMAiRTSDYGN.
PhylomeDBiP0A7V8.

Enzyme and pathway databases

BioCyciEcoCyc:EG10903-MONOMER.
ECOL316407:JW3258-MONOMER.
MetaCyc:EG10903-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7V8.
PROiP0A7V8.

Family and domain databases

Gene3Di1.10.1050.10. 1 hit.
3.10.290.10. 1 hit.
HAMAPiMF_01306_B. Ribosomal_S4_B. 1 hit.
InterProiIPR022801. Ribosomal_S4/S9.
IPR001912. Ribosomal_S4/S9_N.
IPR005709. Ribosomal_S4_bac-type.
IPR018079. Ribosomal_S4_CS.
IPR002942. S4_RNA-bd.
[Graphical view]
PANTHERiPTHR11831. PTHR11831. 1 hit.
PfamiPF00163. Ribosomal_S4. 1 hit.
PF01479. S4. 1 hit.
[Graphical view]
SMARTiSM01390. Ribosomal_S4. 1 hit.
SM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01017. rpsD_bact. 1 hit.
PROSITEiPS00632. RIBOSOMAL_S4. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRS4_ECOLI
AccessioniPrimary (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: November 30, 2016
This is version 127 of the entry and version 2 of the sequence. [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. 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.