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P0AG59

- RS14_ECOLI

UniProt

P0AG59 - RS14_ECOLI

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Protein

30S ribosomal protein S14

Gene

rpsN

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 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

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10913-MONOMER.
ECOL316407:JW3269-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S14
Gene namesi
Name:rpsN
Ordered Locus Names:b3307, JW3269
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10913. rpsN.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic small ribosomal subunit Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 10110030S ribosomal protein S14PRO_0000130890Add
BLAST

Proteomic databases

PaxDbiP0AG59.
PRIDEiP0AG59.

Expressioni

Gene expression databases

GenevestigatoriP0AG59.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Contacts proteins S3 and S10 (By similarity).By similarity

Protein-protein interaction databases

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

Structurei

Secondary structure

1
101
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1916Combined sources
Turni20 – 234Combined sources
Helixi24 – 263Combined sources
Helixi27 – 293Combined sources
Helixi30 – 323Combined sources
Helixi44 – 474Combined sources
Turni49 – 524Combined sources
Helixi53 – 553Combined sources
Helixi57 – 593Combined sources
Turni65 – 673Combined sources
Beta strandi71 – 744Combined sources
Turni75 – 784Combined sources
Helixi81 – 888Combined sources
Turni89 – 913Combined sources
Beta strandi93 – 953Combined sources
Beta strandi96 – 983Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-N42-101[»]
1P6Gelectron microscopy12.30N2-101[»]
1P87electron microscopy11.50N2-101[»]
1VS5X-ray3.46N1-101[»]
1VS7X-ray3.46N1-101[»]
2AVYX-ray3.46N2-101[»]
2AW7X-ray3.46N2-101[»]
2GY9electron microscopy15.00N41-101[»]
2GYBelectron microscopy15.00N41-101[»]
2I2PX-ray3.22N2-101[»]
2I2UX-ray3.22N2-101[»]
2QALX-ray3.21N2-101[»]
2QANX-ray3.21N2-101[»]
2QB9X-ray3.54N2-101[»]
2QBBX-ray3.54N2-101[»]
2QBDX-ray3.30N2-101[»]
2QBFX-ray3.30N2-101[»]
2QBHX-ray4.00N2-101[»]
2QBJX-ray4.00N2-101[»]
2QOUX-ray3.93N2-101[»]
2QOWX-ray3.93N2-101[»]
2QOYX-ray3.50N2-101[»]
2QP0X-ray3.50N2-101[»]
2VHOX-ray3.74N2-101[»]
2VHPX-ray3.74N2-101[»]
2WWLelectron microscopy5.80N2-101[»]
2YKRelectron microscopy9.80N2-101[»]
2Z4KX-ray4.45N2-101[»]
2Z4MX-ray4.45N2-101[»]
3DF1X-ray3.50N2-101[»]
3DF3X-ray3.50N2-101[»]
3E1Aelectron microscopy-G1-101[»]
3E1Celectron microscopy-G1-101[»]
3FIHelectron microscopy6.70N2-101[»]
3I1MX-ray3.19N1-101[»]
3I1OX-ray3.19N1-101[»]
3I1QX-ray3.81N1-101[»]
3I1SX-ray3.81N1-101[»]
3I1ZX-ray3.71N1-101[»]
3I21X-ray3.71N1-101[»]
3IZVelectron microscopy-R1-101[»]
3IZWelectron microscopy-R1-101[»]
3J00electron microscopy-N2-101[»]
3J0Uelectron microscopy12.10Q2-101[»]
3J0Velectron microscopy14.70Q2-101[»]
3J0Xelectron microscopy13.50Q2-101[»]
3J0Zelectron microscopy11.50Q2-101[»]
3J10electron microscopy11.50Q2-101[»]
3J13electron microscopy13.10P2-101[»]
3J18electron microscopy8.30N2-101[»]
3J36electron microscopy9.80N2-101[»]
3J4Velectron microscopy12.00N1-101[»]
3J4Welectron microscopy12.00N1-101[»]
3J4Yelectron microscopy17.00N1-101[»]
3J4Zelectron microscopy20.00N1-101[»]
3J53electron microscopy13.00N1-101[»]
3J55electron microscopy15.00N1-101[»]
3J57electron microscopy17.00N1-101[»]
3J59electron microscopy12.00N1-101[»]
3J5Belectron microscopy17.00N1-101[»]
3J5Delectron microscopy17.00N1-101[»]
3J5Felectron microscopy20.00N1-101[»]
3J5Helectron microscopy15.00N1-101[»]
3J5Jelectron microscopy9.00N1-101[»]
3J5Nelectron microscopy6.80N1-101[»]
3J5Telectron microscopy7.60N2-101[»]
3J5Xelectron microscopy7.60N2-101[»]
3KC4electron microscopy-N1-101[»]
3OAQX-ray3.25N2-101[»]
3OARX-ray3.25N2-101[»]
3OFAX-ray3.19N2-101[»]
3OFBX-ray3.19N2-101[»]
3OFOX-ray3.10N2-101[»]
3OFPX-ray3.10N2-101[»]
3OFXX-ray3.29N2-101[»]
3OFYX-ray3.29N2-101[»]
3OR9X-ray3.30N1-101[»]
3ORAX-ray3.30N1-101[»]
3SFSX-ray3.20N1-101[»]
3UOQX-ray3.70N1-101[»]
4A2Ielectron microscopy16.50N2-101[»]
4ADVelectron microscopy13.50N2-101[»]
4GAQX-ray3.30N1-101[»]
4GASX-ray3.30N1-101[»]
4GD1X-ray3.00N2-101[»]
4GD2X-ray3.00N2-101[»]
4KIYX-ray2.90N1-101[»]
4KJ0X-ray2.90N1-101[»]
4KJ2X-ray2.90N1-101[»]
4KJ4X-ray2.90N1-101[»]
4KJ6X-ray2.90N1-101[»]
4KJ8X-ray2.90N1-101[»]
4KJAX-ray2.90N1-101[»]
4KJCX-ray2.90N1-101[»]
4PE9X-ray2.95N2-101[»]
4PEAX-ray2.95N2-101[»]
4TOLX-ray3.00N2-101[»]
4TONX-ray3.00N2-101[»]
4TOUX-ray2.90N2-101[»]
4TOWX-ray2.90N2-101[»]
4TP0X-ray2.90N2-101[»]
4TP2X-ray2.90N2-101[»]
4TP4X-ray2.90N2-101[»]
4TP6X-ray2.90N2-101[»]
4TP8X-ray2.80N2-101[»]
4TPAX-ray2.80N2-101[»]
4TPCX-ray2.80N2-101[»]
4TPEX-ray2.80N2-101[»]
ProteinModelPortaliP0AG59.
SMRiP0AG59. Positions 2-101.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG59.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S14P family.Curated

Phylogenomic databases

eggNOGiCOG0199.
HOGENOMiHOG000039864.
InParanoidiP0AG59.
KOiK02954.
OMAiRIRNRCW.
OrthoDBiEOG6BCT0K.
PhylomeDBiP0AG59.

Family and domain databases

HAMAPiMF_00537. Ribosomal_S14_1.
InterProiIPR001209. Ribosomal_S14.
IPR023036. Ribosomal_S14_bac/plaastid.
IPR018271. Ribosomal_S14_CS.
[Graphical view]
PANTHERiPTHR19836. PTHR19836. 1 hit.
PfamiPF00253. Ribosomal_S14. 1 hit.
[Graphical view]
PROSITEiPS00527. RIBOSOMAL_S14. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921E → Q AA sequence 1 PublicationCurated
Sequence conflicti99 – 1013ASW → G in CAA25718. (PubMed:6222285)Curated

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.
YP_492125.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76332; AAC76332; b3307.
BAE77984; BAE77984; BAE77984.
GeneIDi12934450.
947801.
KEGGiecj:Y75_p3869.
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 .
PIRi F65123. R3EC14.
RefSeqi NP_417766.1. NC_000913.3.
YP_492125.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M5G model - N 42-101 [» ]
1P6G electron microscopy 12.30 N 2-101 [» ]
1P87 electron microscopy 11.50 N 2-101 [» ]
1VS5 X-ray 3.46 N 1-101 [» ]
1VS7 X-ray 3.46 N 1-101 [» ]
2AVY X-ray 3.46 N 2-101 [» ]
2AW7 X-ray 3.46 N 2-101 [» ]
2GY9 electron microscopy 15.00 N 41-101 [» ]
2GYB electron microscopy 15.00 N 41-101 [» ]
2I2P X-ray 3.22 N 2-101 [» ]
2I2U X-ray 3.22 N 2-101 [» ]
2QAL X-ray 3.21 N 2-101 [» ]
2QAN X-ray 3.21 N 2-101 [» ]
2QB9 X-ray 3.54 N 2-101 [» ]
2QBB X-ray 3.54 N 2-101 [» ]
2QBD X-ray 3.30 N 2-101 [» ]
2QBF X-ray 3.30 N 2-101 [» ]
2QBH X-ray 4.00 N 2-101 [» ]
2QBJ X-ray 4.00 N 2-101 [» ]
2QOU X-ray 3.93 N 2-101 [» ]
2QOW X-ray 3.93 N 2-101 [» ]
2QOY X-ray 3.50 N 2-101 [» ]
2QP0 X-ray 3.50 N 2-101 [» ]
2VHO X-ray 3.74 N 2-101 [» ]
2VHP X-ray 3.74 N 2-101 [» ]
2WWL electron microscopy 5.80 N 2-101 [» ]
2YKR electron microscopy 9.80 N 2-101 [» ]
2Z4K X-ray 4.45 N 2-101 [» ]
2Z4M X-ray 4.45 N 2-101 [» ]
3DF1 X-ray 3.50 N 2-101 [» ]
3DF3 X-ray 3.50 N 2-101 [» ]
3E1A electron microscopy - G 1-101 [» ]
3E1C electron microscopy - G 1-101 [» ]
3FIH electron microscopy 6.70 N 2-101 [» ]
3I1M X-ray 3.19 N 1-101 [» ]
3I1O X-ray 3.19 N 1-101 [» ]
3I1Q X-ray 3.81 N 1-101 [» ]
3I1S X-ray 3.81 N 1-101 [» ]
3I1Z X-ray 3.71 N 1-101 [» ]
3I21 X-ray 3.71 N 1-101 [» ]
3IZV electron microscopy - R 1-101 [» ]
3IZW electron microscopy - R 1-101 [» ]
3J00 electron microscopy - N 2-101 [» ]
3J0U electron microscopy 12.10 Q 2-101 [» ]
3J0V electron microscopy 14.70 Q 2-101 [» ]
3J0X electron microscopy 13.50 Q 2-101 [» ]
3J0Z electron microscopy 11.50 Q 2-101 [» ]
3J10 electron microscopy 11.50 Q 2-101 [» ]
3J13 electron microscopy 13.10 P 2-101 [» ]
3J18 electron microscopy 8.30 N 2-101 [» ]
3J36 electron microscopy 9.80 N 2-101 [» ]
3J4V electron microscopy 12.00 N 1-101 [» ]
3J4W electron microscopy 12.00 N 1-101 [» ]
3J4Y electron microscopy 17.00 N 1-101 [» ]
3J4Z electron microscopy 20.00 N 1-101 [» ]
3J53 electron microscopy 13.00 N 1-101 [» ]
3J55 electron microscopy 15.00 N 1-101 [» ]
3J57 electron microscopy 17.00 N 1-101 [» ]
3J59 electron microscopy 12.00 N 1-101 [» ]
3J5B electron microscopy 17.00 N 1-101 [» ]
3J5D electron microscopy 17.00 N 1-101 [» ]
3J5F electron microscopy 20.00 N 1-101 [» ]
3J5H electron microscopy 15.00 N 1-101 [» ]
3J5J electron microscopy 9.00 N 1-101 [» ]
3J5N electron microscopy 6.80 N 1-101 [» ]
3J5T electron microscopy 7.60 N 2-101 [» ]
3J5X electron microscopy 7.60 N 2-101 [» ]
3KC4 electron microscopy - N 1-101 [» ]
3OAQ X-ray 3.25 N 2-101 [» ]
3OAR X-ray 3.25 N 2-101 [» ]
3OFA X-ray 3.19 N 2-101 [» ]
3OFB X-ray 3.19 N 2-101 [» ]
3OFO X-ray 3.10 N 2-101 [» ]
3OFP X-ray 3.10 N 2-101 [» ]
3OFX X-ray 3.29 N 2-101 [» ]
3OFY X-ray 3.29 N 2-101 [» ]
3OR9 X-ray 3.30 N 1-101 [» ]
3ORA X-ray 3.30 N 1-101 [» ]
3SFS X-ray 3.20 N 1-101 [» ]
3UOQ X-ray 3.70 N 1-101 [» ]
4A2I electron microscopy 16.50 N 2-101 [» ]
4ADV electron microscopy 13.50 N 2-101 [» ]
4GAQ X-ray 3.30 N 1-101 [» ]
4GAS X-ray 3.30 N 1-101 [» ]
4GD1 X-ray 3.00 N 2-101 [» ]
4GD2 X-ray 3.00 N 2-101 [» ]
4KIY X-ray 2.90 N 1-101 [» ]
4KJ0 X-ray 2.90 N 1-101 [» ]
4KJ2 X-ray 2.90 N 1-101 [» ]
4KJ4 X-ray 2.90 N 1-101 [» ]
4KJ6 X-ray 2.90 N 1-101 [» ]
4KJ8 X-ray 2.90 N 1-101 [» ]
4KJA X-ray 2.90 N 1-101 [» ]
4KJC X-ray 2.90 N 1-101 [» ]
4PE9 X-ray 2.95 N 2-101 [» ]
4PEA X-ray 2.95 N 2-101 [» ]
4TOL X-ray 3.00 N 2-101 [» ]
4TON X-ray 3.00 N 2-101 [» ]
4TOU X-ray 2.90 N 2-101 [» ]
4TOW X-ray 2.90 N 2-101 [» ]
4TP0 X-ray 2.90 N 2-101 [» ]
4TP2 X-ray 2.90 N 2-101 [» ]
4TP4 X-ray 2.90 N 2-101 [» ]
4TP6 X-ray 2.90 N 2-101 [» ]
4TP8 X-ray 2.80 N 2-101 [» ]
4TPA X-ray 2.80 N 2-101 [» ]
4TPC X-ray 2.80 N 2-101 [» ]
4TPE X-ray 2.80 N 2-101 [» ]
ProteinModelPortali P0AG59.
SMRi P0AG59. Positions 2-101.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35805N.
IntActi P0AG59. 70 interactions.
MINTi MINT-1295909.
STRINGi 511145.b3307.

Chemistry

ChEMBLi CHEMBL2363135.
DrugBanki DB00759. Tetracycline.
DB00560. Tigecycline.

Proteomic databases

PaxDbi P0AG59.
PRIDEi P0AG59.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76332 ; AAC76332 ; b3307 .
BAE77984 ; BAE77984 ; BAE77984 .
GeneIDi 12934450.
947801.
KEGGi ecj:Y75_p3869.
eco:b3307.
PATRICi 32122046. VBIEscCol129921_3400.

Organism-specific databases

EchoBASEi EB0906.
EcoGenei EG10913. rpsN.

Phylogenomic databases

eggNOGi COG0199.
HOGENOMi HOG000039864.
InParanoidi P0AG59.
KOi K02954.
OMAi RIRNRCW.
OrthoDBi EOG6BCT0K.
PhylomeDBi P0AG59.

Enzyme and pathway databases

BioCyci EcoCyc:EG10913-MONOMER.
ECOL316407:JW3269-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AG59.
PROi P0AG59.

Gene expression databases

Genevestigatori P0AG59.

Family and domain databases

HAMAPi MF_00537. Ribosomal_S14_1.
InterProi IPR001209. Ribosomal_S14.
IPR023036. Ribosomal_S14_bac/plaastid.
IPR018271. Ribosomal_S14_CS.
[Graphical view ]
PANTHERi PTHR19836. PTHR19836. 1 hit.
Pfami PF00253. Ribosomal_S14. 1 hit.
[Graphical view ]
PROSITEi PS00527. RIBOSOMAL_S14. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Yaguchi M., Roy C., Reithmeier R.A.F., Wittmann-Liebold B.
    Submitted (OCT-1982) to the PIR data bank
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-101.
    Strain: K12.
  2. "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
    Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
    Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  6. "All-atom homology model of the Escherichia coli 30S ribosomal subunit."
    Tung C.-S., Joseph S., Sanbonmatsu K.Y.
    Nat. Struct. Biol. 9:750-755(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  7. "Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
    Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
    Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
    Strain: MRE-600.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS14_ECOLI
AccessioniPrimary (citable) accession number: P0AG59
Secondary accession number(s): P02370, Q2M6X2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 93 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

External Data

Dasty 3