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Protein

30S ribosomal protein S14

Gene

rpsN

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

  • structural constituent of ribosome Source: CAFA

GO - Biological processi

  • ribosomal small subunit assembly Source: CAFA
  • translation Source: GO_Central

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

  • cytosolic small ribosomal subunit Source: CAFA

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. 70 interactors.
MINTiMINT-1295909.
STRINGi511145.b3307.

Structurei

Secondary structure

1101
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 19Combined sources16
Turni20 – 23Combined sources4
Helixi24 – 26Combined sources3
Helixi27 – 29Combined sources3
Helixi30 – 32Combined sources3
Helixi44 – 47Combined sources4
Turni49 – 52Combined sources4
Helixi53 – 55Combined sources3
Helixi57 – 59Combined sources3
Turni65 – 67Combined sources3
Beta strandi71 – 74Combined sources4
Turni75 – 78Combined sources4
Helixi81 – 88Combined sources8
Turni89 – 91Combined sources3
Beta strandi93 – 95Combined sources3
Beta strandi96 – 98Combined sources3

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[»]
5U4Ielectron microscopy3.50n2-101[»]
ProteinModelPortaliP0AG59.
SMRiP0AG59.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG59.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105VBI. Bacteria.
COG0199. LUCA.
HOGENOMiHOG000039864.
InParanoidiP0AG59.
KOiK02954.
OMAiGVYSKFG.
PhylomeDBiP0AG59.

Family and domain databases

HAMAPiMF_00537. Ribosomal_S14_1. 1 hit.
InterProiView protein in InterPro
IPR001209. Ribosomal_S14.
IPR023036. Ribosomal_S14_bac/plaastid.
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.
PATRICi32122046. VBIEscCol129921_3400.

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[»]
5U4Ielectron microscopy3.50n2-101[»]
ProteinModelPortaliP0AG59.
SMRiP0AG59.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35805N.
IntActiP0AG59. 70 interactors.
MINTiMINT-1295909.
STRINGi511145.b3307.

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.
PATRICi32122046. VBIEscCol129921_3400.

Organism-specific databases

EchoBASEiEB0906.
EcoGeneiEG10913. rpsN.

Phylogenomic databases

eggNOGiENOG4105VBI. Bacteria.
COG0199. LUCA.
HOGENOMiHOG000039864.
InParanoidiP0AG59.
KOiK02954.
OMAiGVYSKFG.
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/plaastid.
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: May 10, 2017
This is version 115 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. 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.