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Protein

30S ribosomal protein S14

Gene

rpsN

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

Functioni

Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.

GO - Molecular functioni

  • rRNA binding Source: UniProtKB-UniRule
  • structural constituent of ribosome Source: CAFA

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10913-MONOMER
MetaCyc:EG10913-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S14
Alternative name(s):
Small ribosomal subunit protein uS141 Publication
Gene namesi
Name:rpsN
Ordered Locus Names:b3307, JW3269
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10913 rpsN

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Chemistry databases

DrugBankiDB00759 Tetracycline
DB00560 Tigecycline

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001308902 – 10130S ribosomal protein S14Add BLAST100

Proteomic databases

EPDiP0AG59
PaxDbiP0AG59
PRIDEiP0AG59

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit (PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:12244297, PubMed:27906160, PubMed:27906161). Contacts proteins S3 and S10 (By similarity).UniRule annotation7 Publications

Protein-protein interaction databases

DIPiDIP-35805N
IntActiP0AG59, 82 interactors
STRINGi316385.ECDH10B_3482

Structurei

Secondary structure

1101
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0AG59
SMRiP0AG59
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG59

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105VBI Bacteria
COG0199 LUCA
HOGENOMiHOG000039864
InParanoidiP0AG59
KOiK02954
PhylomeDBiP0AG59

Family and domain databases

HAMAPiMF_00537 Ribosomal_S14_1, 1 hit
InterProiView protein in InterPro
IPR001209 Ribosomal_S14
IPR023036 Ribosomal_S14_bac/plastid
IPR018271 Ribosomal_S14_CS
PANTHERiPTHR19836 PTHR19836, 1 hit
PfamiView protein in Pfam
PF00253 Ribosomal_S14, 1 hit
PROSITEiView protein in PROSITE
PS00527 RIBOSOMAL_S14, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0AG59-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKQSMKARE VKRVALADKY FAKRAELKAI ISDVNASDED RWNAVLKLQT
60 70 80 90 100
LPRDSSPSRQ RNRCRQTGRP HGFLRKFGLS RIKVREAAMR GEIPGLKKAS

W
Length:101
Mass (Da):11,580
Last modified:January 23, 2007 - v2
Checksum:iE2B21D9D3752352C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti92E → Q AA sequence (Ref. 1) Curated1
Sequence conflicti99 – 101ASW → G in CAA25718 (PubMed:6222285).Curated3

Mass spectrometryi

Molecular mass is 11449.3 Da from positions 2 - 101. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA Translation: CAA25718.1
U18997 Genomic DNA Translation: AAA58104.1
U00096 Genomic DNA Translation: AAC76332.1
AP009048 Genomic DNA Translation: BAE77984.1
PIRiF65123 R3EC14
RefSeqiNP_417766.1, NC_000913.3
WP_001118930.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76332; AAC76332; b3307
BAE77984; BAE77984; BAE77984
GeneIDi947801
KEGGiecj:JW3269
eco:b3307
PATRICifig|1411691.4.peg.3424

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA Translation: CAA25718.1
U18997 Genomic DNA Translation: AAA58104.1
U00096 Genomic DNA Translation: AAC76332.1
AP009048 Genomic DNA Translation: BAE77984.1
PIRiF65123 R3EC14
RefSeqiNP_417766.1, NC_000913.3
WP_001118930.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-N42-101[»]
2YKRelectron microscopy9.80N2-101[»]
3J9Yelectron microscopy3.90n1-101[»]
3J9Zelectron microscopy3.60SN2-101[»]
3JA1electron microscopy3.60SN2-101[»]
3JBUelectron microscopy3.64N1-101[»]
3JBVelectron microscopy3.32N1-101[»]
3JCDelectron microscopy3.70n1-101[»]
3JCEelectron microscopy3.20n1-101[»]
3JCJelectron microscopy3.70w1-101[»]
3JCNelectron microscopy4.60q1-101[»]
4A2Ielectron microscopy16.50N2-101[»]
4ADVelectron microscopy13.50N2-101[»]
4U1UX-ray2.95AN/CN2-101[»]
4U1VX-ray3.00AN/CN2-101[»]
4U20X-ray2.90AN/CN2-101[»]
4U24X-ray2.90AN/CN2-101[»]
4U25X-ray2.90AN/CN2-101[»]
4U26X-ray2.80AN/CN2-101[»]
4U27X-ray2.80AN/CN2-101[»]
4V47electron microscopy12.30BN2-101[»]
4V48electron microscopy11.50BN2-101[»]
4V4HX-ray3.46AN/CN1-101[»]
4V4QX-ray3.46AN/CN2-101[»]
4V4Velectron microscopy15.00AN41-101[»]
4V4Welectron microscopy15.00AN41-101[»]
4V50X-ray3.22AN/CN2-101[»]
4V52X-ray3.21AN/CN2-101[»]
4V53X-ray3.54AN/CN2-101[»]
4V54X-ray3.30AN/CN2-101[»]
4V55X-ray4.00AN/CN2-101[»]
4V56X-ray3.93AN/CN2-101[»]
4V57X-ray3.50AN/CN2-101[»]
4V5BX-ray3.74BN/DN2-101[»]
4V5Helectron microscopy5.80AN2-101[»]
4V5YX-ray4.45AN/CN2-101[»]
4V64X-ray3.50AN/CN2-101[»]
4V65electron microscopy9.00AG1-101[»]
4V66electron microscopy9.00AG1-101[»]
4V69electron microscopy6.70AN2-101[»]
4V6CX-ray3.19AN/CN1-101[»]
4V6DX-ray3.81AN/CN1-101[»]
4V6EX-ray3.71AN/CN1-101[»]
4V6Kelectron microscopy8.25BR1-101[»]
4V6Lelectron microscopy13.20AR1-101[»]
4V6Melectron microscopy7.10AN2-101[»]
4V6Nelectron microscopy12.10BQ2-101[»]
4V6Oelectron microscopy14.70AQ2-101[»]
4V6Pelectron microscopy13.50AQ2-101[»]
4V6Qelectron microscopy11.50AQ2-101[»]
4V6Relectron microscopy11.50AQ2-101[»]
4V6Selectron microscopy13.10BP2-101[»]
4V6Telectron microscopy8.30AN2-101[»]
4V6Velectron microscopy9.80AN2-101[»]
4V6Yelectron microscopy12.00AN1-101[»]
4V6Zelectron microscopy12.00AN1-101[»]
4V70electron microscopy17.00AN1-101[»]
4V71electron microscopy20.00AN1-101[»]
4V72electron microscopy13.00AN1-101[»]
4V73electron microscopy15.00AN1-101[»]
4V74electron microscopy17.00AN1-101[»]
4V75electron microscopy12.00AN1-101[»]
4V76electron microscopy17.00AN1-101[»]
4V77electron microscopy17.00AN1-101[»]
4V78electron microscopy20.00AN1-101[»]
4V79electron microscopy15.00AN1-101[»]
4V7Aelectron microscopy9.00AN1-101[»]
4V7Belectron microscopy6.80AN1-101[»]
4V7Celectron microscopy7.60AN2-101[»]
4V7Delectron microscopy7.60BN2-101[»]
4V7Ielectron microscopy9.60BN1-101[»]
4V7SX-ray3.25AN/CN2-101[»]
4V7TX-ray3.19AN/CN2-101[»]
4V7UX-ray3.10AN/CN2-101[»]
4V7VX-ray3.29AN/CN2-101[»]
4V85X-ray3.20N1-101[»]
4V89X-ray3.70AN1-101[»]
4V9CX-ray3.30AN/CN1-101[»]
4V9DX-ray3.00AN/BN2-101[»]
4V9OX-ray2.90BN/DN/FN/HN1-101[»]
4V9PX-ray2.90BN/DN/FN/HN1-101[»]
4WF1X-ray3.09AN/CN2-101[»]
4WOIX-ray3.00AN/DN1-101[»]
4WWWX-ray3.10QN/XN1-101[»]
4YBBX-ray2.10AN/BN2-101[»]
5AFIelectron microscopy2.90n1-101[»]
5H5Uelectron microscopy3.00u2-101[»]
5IQRelectron microscopy3.00s1-101[»]
5IT8X-ray3.12AN/BN2-101[»]
5J5BX-ray2.80AN/BN2-101[»]
5J7LX-ray3.00AN/BN2-101[»]
5J88X-ray3.32AN/BN2-101[»]
5J8AX-ray3.10AN/BN2-101[»]
5J91X-ray2.96AN/BN2-101[»]
5JC9X-ray3.03AN/BN2-101[»]
5JTEelectron microscopy3.60AN1-101[»]
5JU8electron microscopy3.60AN1-101[»]
5KCRelectron microscopy3.601n1-101[»]
5KCSelectron microscopy3.901n1-101[»]
5KPSelectron microscopy3.90191-101[»]
5KPVelectron microscopy4.10181-101[»]
5KPWelectron microscopy3.90181-101[»]
5KPXelectron microscopy3.90181-101[»]
5L3Pelectron microscopy3.70n1-101[»]
5LZAelectron microscopy3.60n2-101[»]
5LZBelectron microscopy5.30n2-101[»]
5LZCelectron microscopy4.80n2-101[»]
5LZDelectron microscopy3.40n2-101[»]
5LZEelectron microscopy3.50n2-101[»]
5LZFelectron microscopy4.60n2-101[»]
5MDVelectron microscopy2.97s1-101[»]
5MDWelectron microscopy3.06s1-101[»]
5MDYelectron microscopy3.35s1-101[»]
5MDZelectron microscopy3.10s1-101[»]
5ME0electron microscopy13.50N1-101[»]
5ME1electron microscopy13.50N1-101[»]
5MGPelectron microscopy3.10n2-101[»]
5MY1electron microscopy7.60N2-101[»]
5NO2electron microscopy5.16N2-101[»]
5NO3electron microscopy5.16N2-101[»]
5NO4electron microscopy5.16N2-101[»]
5NP6electron microscopy3.60Q2-101[»]
5NWYelectron microscopy2.93D1-101[»]
5O2Relectron microscopy3.40n2-101[»]
5U4Ielectron microscopy3.50n2-101[»]
5U9Felectron microscopy3.20N1-101[»]
5U9Gelectron microscopy3.20N1-101[»]
5UYKelectron microscopy3.90N2-101[»]
5UYLelectron microscopy3.60N2-101[»]
5UYMelectron microscopy3.20N2-101[»]
5UYNelectron microscopy4.00N2-101[»]
5UYPelectron microscopy3.90N2-101[»]
5UYQelectron microscopy3.80N2-101[»]
5UZ4electron microscopy5.80N1-101[»]
5WDTelectron microscopy3.00n2-101[»]
5WE4electron microscopy3.10n2-101[»]
5WE6electron microscopy3.40n2-101[»]
5WFKelectron microscopy3.40n2-101[»]
6BU8electron microscopy3.50N2-101[»]
6C4Ielectron microscopy3.24n1-101[»]
6ENFelectron microscopy3.20n2-101[»]
6ENJelectron microscopy3.70n2-101[»]
6ENUelectron microscopy3.10n2-101[»]
6GWTelectron microscopy3.80n2-101[»]
6GXMelectron microscopy3.80n2-101[»]
6GXNelectron microscopy3.90n2-101[»]
6GXOelectron microscopy3.90n2-101[»]
6GXPelectron microscopy4.40n2-101[»]
6H4Nelectron microscopy3.00n2-101[»]
6H58electron microscopy7.90n/nn2-101[»]
ProteinModelPortaliP0AG59
SMRiP0AG59
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35805N
IntActiP0AG59, 82 interactors
STRINGi316385.ECDH10B_3482

Chemistry databases

DrugBankiDB00759 Tetracycline
DB00560 Tigecycline

Proteomic databases

EPDiP0AG59
PaxDbiP0AG59
PRIDEiP0AG59

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76332; AAC76332; b3307
BAE77984; BAE77984; BAE77984
GeneIDi947801
KEGGiecj:JW3269
eco:b3307
PATRICifig|1411691.4.peg.3424

Organism-specific databases

EchoBASEiEB0906
EcoGeneiEG10913 rpsN

Phylogenomic databases

eggNOGiENOG4105VBI Bacteria
COG0199 LUCA
HOGENOMiHOG000039864
InParanoidiP0AG59
KOiK02954
PhylomeDBiP0AG59

Enzyme and pathway databases

BioCyciEcoCyc:EG10913-MONOMER
MetaCyc:EG10913-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0AG59
PROiPR:P0AG59

Family and domain databases

HAMAPiMF_00537 Ribosomal_S14_1, 1 hit
InterProiView protein in InterPro
IPR001209 Ribosomal_S14
IPR023036 Ribosomal_S14_bac/plastid
IPR018271 Ribosomal_S14_CS
PANTHERiPTHR19836 PTHR19836, 1 hit
PfamiView protein in Pfam
PF00253 Ribosomal_S14, 1 hit
PROSITEiView protein in PROSITE
PS00527 RIBOSOMAL_S14, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRS14_ECOLI
AccessioniPrimary (citable) accession number: P0AG59
Secondary accession number(s): P02370, Q2M6X2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 126 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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