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Protein

30S ribosomal protein S10

Gene

rpsJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the binding of tRNA to the ribosomes.

GO - Molecular functioni

  1. structural constituent of ribosome Source: GO_Central
  2. tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. translation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10909-MONOMER.
ECOL316407:JW3283-MONOMER.

Protein family/group databases

MoonProtiP0A7R5.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S10
Gene namesi
Name:rpsJ
Synonyms:nusE
Ordered Locus Names:b3321, JW3283
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10909. rpsJ.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10310330S ribosomal protein S10PRO_0000146529Add
BLAST

Proteomic databases

PaxDbiP0A7R5.
PRIDEiP0A7R5.

Expressioni

Gene expression databases

GenevestigatoriP0A7R5.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
nusBP0A7805EBI-544602,EBI-555387
rsuAP0AA432EBI-544602,EBI-557810

Protein-protein interaction databases

BioGridi852128. 1 interaction.
DIPiDIP-35797N.
IntActiP0A7R5. 98 interactions.
MINTiMINT-1283940.
STRINGi511145.b3321.

Structurei

Secondary structure

1
103
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139Combined sources
Helixi15 – 3016Combined sources
Turni31 – 333Combined sources
Beta strandi35 – 4511Combined sources
Beta strandi46 – 516Combined sources
Beta strandi54 – 574Combined sources
Beta strandi63 – 686Combined sources
Beta strandi69 – 7810Combined sources
Helixi81 – 899Combined sources
Beta strandi96 – 1038Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-J5-102[»]
1P6Gelectron microscopy12.30J1-103[»]
1P87electron microscopy11.50J1-103[»]
1VS5X-ray3.46J1-103[»]
1VS7X-ray3.46J1-103[»]
2AVYX-ray3.46J1-103[»]
2AW7X-ray3.46J1-103[»]
2GY9electron microscopy15.00J5-100[»]
2GYBelectron microscopy15.00J5-100[»]
2I2PX-ray3.22J1-103[»]
2I2UX-ray3.22J1-103[»]
2KVQNMR-E1-45[»]
E68-103[»]
2QALX-ray3.21J1-103[»]
2QANX-ray3.21J1-103[»]
2QB9X-ray3.54J1-103[»]
2QBBX-ray3.54J1-103[»]
2QBDX-ray3.30J1-103[»]
2QBFX-ray3.30J1-103[»]
2QBHX-ray4.00J1-103[»]
2QBJX-ray4.00J1-103[»]
2QOUX-ray3.93J1-103[»]
2QOWX-ray3.93J1-103[»]
2QOYX-ray3.50J1-103[»]
2QP0X-ray3.50J1-103[»]
2VHOX-ray3.74J1-103[»]
2VHPX-ray3.74J1-103[»]
2WWLelectron microscopy5.80J5-102[»]
2YKRelectron microscopy9.80J5-102[»]
2Z4KX-ray4.45J1-103[»]
2Z4MX-ray4.45J1-103[»]
3D3BX-ray1.30J1-45[»]
J68-103[»]
3D3CX-ray2.60J/K/L1-45[»]
J/K/L68-103[»]
3DF1X-ray3.50J1-103[»]
3DF3X-ray3.50J1-103[»]
3E1Aelectron microscopy-X1-103[»]
3E1Celectron microscopy-X1-103[»]
3FIHelectron microscopy6.70J5-102[»]
3I1MX-ray3.19J1-103[»]
3I1OX-ray3.19J1-103[»]
3I1QX-ray3.81J1-103[»]
3I1SX-ray3.81J1-103[»]
3I1ZX-ray3.71J1-103[»]
3I21X-ray3.71J1-103[»]
3IMQX-ray2.50J/K/L1-103[»]
3IZVelectron microscopy-N1-103[»]
3IZWelectron microscopy-N1-103[»]
3J00electron microscopy-J1-103[»]
3J0Uelectron microscopy12.10M1-103[»]
3J0Velectron microscopy14.70M1-103[»]
3J0Xelectron microscopy13.50M1-103[»]
3J0Zelectron microscopy11.50M1-103[»]
3J10electron microscopy11.50M1-103[»]
3J13electron microscopy13.10L1-103[»]
3J18electron microscopy8.30J5-102[»]
3J36electron microscopy9.80J1-103[»]
3J4Velectron microscopy12.00J5-102[»]
3J4Welectron microscopy12.00J5-102[»]
3J4Yelectron microscopy17.00J5-102[»]
3J4Zelectron microscopy20.00J5-102[»]
3J53electron microscopy13.00J5-102[»]
3J55electron microscopy15.00J5-102[»]
3J57electron microscopy17.00J5-102[»]
3J59electron microscopy12.00J5-102[»]
3J5Belectron microscopy17.00J5-102[»]
3J5Delectron microscopy17.00J5-102[»]
3J5Felectron microscopy20.00J5-102[»]
3J5Helectron microscopy15.00J5-102[»]
3J5Jelectron microscopy9.00J5-102[»]
3J5Nelectron microscopy6.80J1-103[»]
3J5Telectron microscopy7.60J1-103[»]
3J5Xelectron microscopy7.60J1-103[»]
3KC4electron microscopy-J1-103[»]
3OAQX-ray3.25J5-102[»]
3OARX-ray3.25J5-102[»]
3OFAX-ray3.19J5-102[»]
3OFBX-ray3.19J5-102[»]
3OFOX-ray3.10J5-102[»]
3OFPX-ray3.10J5-102[»]
3OFXX-ray3.29J5-102[»]
3OFYX-ray3.29J5-102[»]
3OR9X-ray3.30J1-103[»]
3ORAX-ray3.30J1-103[»]
3SFSX-ray3.20J1-103[»]
3UOQX-ray3.70J1-103[»]
3W1YX-ray2.30C1-103[»]
4A2Ielectron microscopy16.50J5-102[»]
4ADVelectron microscopy13.50J1-103[»]
4GAQX-ray3.30J1-103[»]
4GASX-ray3.30J1-103[»]
4GD1X-ray3.00J5-102[»]
4GD2X-ray3.00J5-102[»]
4KIYX-ray2.90J1-103[»]
4KJ0X-ray2.90J1-103[»]
4KJ2X-ray2.90J1-103[»]
4KJ4X-ray2.90J1-103[»]
4KJ6X-ray2.90J1-103[»]
4KJ8X-ray2.90J1-103[»]
4KJAX-ray2.90J1-103[»]
4KJCX-ray2.90J1-103[»]
4PE9X-ray2.95J5-102[»]
4PEAX-ray2.95J5-102[»]
4TOLX-ray3.00J5-102[»]
4TONX-ray3.00J5-102[»]
4TOUX-ray2.90J5-102[»]
4TOWX-ray2.90J5-102[»]
4TP0X-ray2.90J5-102[»]
4TP2X-ray2.90J5-102[»]
4TP4X-ray2.90J5-102[»]
4TP6X-ray2.90J5-102[»]
4TP8X-ray2.80J5-102[»]
4TPAX-ray2.80J5-102[»]
4TPCX-ray2.80J5-102[»]
4TPEX-ray2.80J5-102[»]
4WAOX-ray3.09J5-102[»]
4WAQX-ray3.09J5-102[»]
ProteinModelPortaliP0A7R5.
SMRiP0A7R5. Positions 5-100.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7R5.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S10P family.Curated

Phylogenomic databases

eggNOGiCOG0051.
HOGENOMiHOG000270246.
InParanoidiP0A7R5.
KOiK02946.
OMAiIESLMHI.
OrthoDBiEOG6VXFHB.
PhylomeDBiP0A7R5.

Family and domain databases

Gene3Di3.30.70.600. 1 hit.
HAMAPiMF_00508. Ribosomal_S10.
InterProiIPR001848. Ribosomal_S10.
IPR018268. Ribosomal_S10_CS.
IPR027486. Ribosomal_S10_dom.
[Graphical view]
PANTHERiPTHR11700. PTHR11700. 1 hit.
PfamiPF00338. Ribosomal_S10. 1 hit.
[Graphical view]
PRINTSiPR00971. RIBOSOMALS10.
SUPFAMiSSF54999. SSF54999. 1 hit.
TIGRFAMsiTIGR01049. rpsJ_bact. 1 hit.
PROSITEiPS00361. RIBOSOMAL_S10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A7R5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQNQRIRIRL KAFDHRLIDQ ATAEIVETAK RTGAQVRGPI PLPTRKERFT
60 70 80 90 100
VLISPHVNKD ARDQYEIRTH LRLVDIVEPT EKTVDALMRL DLAAGVDVQI

SLG
Length:103
Mass (Da):11,736
Last modified:July 21, 1986 - v1
Checksum:iDAEB35A2557F1D59
GO

Mass spectrometryi

Molecular mass is 11734.5 Da from positions 1 - 103. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00344 Genomic DNA. Translation: CAA23633.1.
X02613 Genomic DNA. Translation: CAA26459.1.
U18997 Genomic DNA. Translation: AAA58118.1.
U00096 Genomic DNA. Translation: AAC76346.1.
AP009048 Genomic DNA. Translation: BAE77970.1.
AF058450 Genomic DNA. Translation: AAC14290.1.
PIRiA02720. R3EC10.
RefSeqiNP_417780.1. NC_000913.3.
YP_492111.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76346; AAC76346; b3321.
BAE77970; BAE77970; BAE77970.
GeneIDi12932299.
947816.
KEGGiecj:Y75_p3855.
eco:b3321.
PATRICi32122074. VBIEscCol129921_3414.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00344 Genomic DNA. Translation: CAA23633.1.
X02613 Genomic DNA. Translation: CAA26459.1.
U18997 Genomic DNA. Translation: AAA58118.1.
U00096 Genomic DNA. Translation: AAC76346.1.
AP009048 Genomic DNA. Translation: BAE77970.1.
AF058450 Genomic DNA. Translation: AAC14290.1.
PIRiA02720. R3EC10.
RefSeqiNP_417780.1. NC_000913.3.
YP_492111.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-J5-102[»]
1P6Gelectron microscopy12.30J1-103[»]
1P87electron microscopy11.50J1-103[»]
1VS5X-ray3.46J1-103[»]
1VS7X-ray3.46J1-103[»]
2AVYX-ray3.46J1-103[»]
2AW7X-ray3.46J1-103[»]
2GY9electron microscopy15.00J5-100[»]
2GYBelectron microscopy15.00J5-100[»]
2I2PX-ray3.22J1-103[»]
2I2UX-ray3.22J1-103[»]
2KVQNMR-E1-45[»]
E68-103[»]
2QALX-ray3.21J1-103[»]
2QANX-ray3.21J1-103[»]
2QB9X-ray3.54J1-103[»]
2QBBX-ray3.54J1-103[»]
2QBDX-ray3.30J1-103[»]
2QBFX-ray3.30J1-103[»]
2QBHX-ray4.00J1-103[»]
2QBJX-ray4.00J1-103[»]
2QOUX-ray3.93J1-103[»]
2QOWX-ray3.93J1-103[»]
2QOYX-ray3.50J1-103[»]
2QP0X-ray3.50J1-103[»]
2VHOX-ray3.74J1-103[»]
2VHPX-ray3.74J1-103[»]
2WWLelectron microscopy5.80J5-102[»]
2YKRelectron microscopy9.80J5-102[»]
2Z4KX-ray4.45J1-103[»]
2Z4MX-ray4.45J1-103[»]
3D3BX-ray1.30J1-45[»]
J68-103[»]
3D3CX-ray2.60J/K/L1-45[»]
J/K/L68-103[»]
3DF1X-ray3.50J1-103[»]
3DF3X-ray3.50J1-103[»]
3E1Aelectron microscopy-X1-103[»]
3E1Celectron microscopy-X1-103[»]
3FIHelectron microscopy6.70J5-102[»]
3I1MX-ray3.19J1-103[»]
3I1OX-ray3.19J1-103[»]
3I1QX-ray3.81J1-103[»]
3I1SX-ray3.81J1-103[»]
3I1ZX-ray3.71J1-103[»]
3I21X-ray3.71J1-103[»]
3IMQX-ray2.50J/K/L1-103[»]
3IZVelectron microscopy-N1-103[»]
3IZWelectron microscopy-N1-103[»]
3J00electron microscopy-J1-103[»]
3J0Uelectron microscopy12.10M1-103[»]
3J0Velectron microscopy14.70M1-103[»]
3J0Xelectron microscopy13.50M1-103[»]
3J0Zelectron microscopy11.50M1-103[»]
3J10electron microscopy11.50M1-103[»]
3J13electron microscopy13.10L1-103[»]
3J18electron microscopy8.30J5-102[»]
3J36electron microscopy9.80J1-103[»]
3J4Velectron microscopy12.00J5-102[»]
3J4Welectron microscopy12.00J5-102[»]
3J4Yelectron microscopy17.00J5-102[»]
3J4Zelectron microscopy20.00J5-102[»]
3J53electron microscopy13.00J5-102[»]
3J55electron microscopy15.00J5-102[»]
3J57electron microscopy17.00J5-102[»]
3J59electron microscopy12.00J5-102[»]
3J5Belectron microscopy17.00J5-102[»]
3J5Delectron microscopy17.00J5-102[»]
3J5Felectron microscopy20.00J5-102[»]
3J5Helectron microscopy15.00J5-102[»]
3J5Jelectron microscopy9.00J5-102[»]
3J5Nelectron microscopy6.80J1-103[»]
3J5Telectron microscopy7.60J1-103[»]
3J5Xelectron microscopy7.60J1-103[»]
3KC4electron microscopy-J1-103[»]
3OAQX-ray3.25J5-102[»]
3OARX-ray3.25J5-102[»]
3OFAX-ray3.19J5-102[»]
3OFBX-ray3.19J5-102[»]
3OFOX-ray3.10J5-102[»]
3OFPX-ray3.10J5-102[»]
3OFXX-ray3.29J5-102[»]
3OFYX-ray3.29J5-102[»]
3OR9X-ray3.30J1-103[»]
3ORAX-ray3.30J1-103[»]
3SFSX-ray3.20J1-103[»]
3UOQX-ray3.70J1-103[»]
3W1YX-ray2.30C1-103[»]
4A2Ielectron microscopy16.50J5-102[»]
4ADVelectron microscopy13.50J1-103[»]
4GAQX-ray3.30J1-103[»]
4GASX-ray3.30J1-103[»]
4GD1X-ray3.00J5-102[»]
4GD2X-ray3.00J5-102[»]
4KIYX-ray2.90J1-103[»]
4KJ0X-ray2.90J1-103[»]
4KJ2X-ray2.90J1-103[»]
4KJ4X-ray2.90J1-103[»]
4KJ6X-ray2.90J1-103[»]
4KJ8X-ray2.90J1-103[»]
4KJAX-ray2.90J1-103[»]
4KJCX-ray2.90J1-103[»]
4PE9X-ray2.95J5-102[»]
4PEAX-ray2.95J5-102[»]
4TOLX-ray3.00J5-102[»]
4TONX-ray3.00J5-102[»]
4TOUX-ray2.90J5-102[»]
4TOWX-ray2.90J5-102[»]
4TP0X-ray2.90J5-102[»]
4TP2X-ray2.90J5-102[»]
4TP4X-ray2.90J5-102[»]
4TP6X-ray2.90J5-102[»]
4TP8X-ray2.80J5-102[»]
4TPAX-ray2.80J5-102[»]
4TPCX-ray2.80J5-102[»]
4TPEX-ray2.80J5-102[»]
4WAOX-ray3.09J5-102[»]
4WAQX-ray3.09J5-102[»]
ProteinModelPortaliP0A7R5.
SMRiP0A7R5. Positions 5-100.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852128. 1 interaction.
DIPiDIP-35797N.
IntActiP0A7R5. 98 interactions.
MINTiMINT-1283940.
STRINGi511145.b3321.

Chemistry

ChEMBLiCHEMBL2363135.
DrugBankiDB00698. Nitrofurantoin.

Protein family/group databases

MoonProtiP0A7R5.

Proteomic databases

PaxDbiP0A7R5.
PRIDEiP0A7R5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76346; AAC76346; b3321.
BAE77970; BAE77970; BAE77970.
GeneIDi12932299.
947816.
KEGGiecj:Y75_p3855.
eco:b3321.
PATRICi32122074. VBIEscCol129921_3414.

Organism-specific databases

EchoBASEiEB0902.
EcoGeneiEG10909. rpsJ.

Phylogenomic databases

eggNOGiCOG0051.
HOGENOMiHOG000270246.
InParanoidiP0A7R5.
KOiK02946.
OMAiIESLMHI.
OrthoDBiEOG6VXFHB.
PhylomeDBiP0A7R5.

Enzyme and pathway databases

BioCyciEcoCyc:EG10909-MONOMER.
ECOL316407:JW3283-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7R5.
PROiP0A7R5.

Gene expression databases

GenevestigatoriP0A7R5.

Family and domain databases

Gene3Di3.30.70.600. 1 hit.
HAMAPiMF_00508. Ribosomal_S10.
InterProiIPR001848. Ribosomal_S10.
IPR018268. Ribosomal_S10_CS.
IPR027486. Ribosomal_S10_dom.
[Graphical view]
PANTHERiPTHR11700. PTHR11700. 1 hit.
PfamiPF00338. Ribosomal_S10. 1 hit.
[Graphical view]
PRINTSiPR00971. RIBOSOMALS10.
SUPFAMiSSF54999. SSF54999. 1 hit.
TIGRFAMsiTIGR01049. rpsJ_bact. 1 hit.
PROSITEiPS00361. RIBOSOMAL_S10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of protein S10 from the small ribosomal subunit of Escherichia coli."
    Yaguchi M., Roy C., Wittmann H.G.
    FEBS Lett. 121:113-116(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Regulation of the S10 ribosomal protein operon in E. coli: nucleotide sequence at the start of the operon."
    Olins P.O., Nomura M.
    Cell 26:205-211(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Structure of the Escherichia coli S10 ribosomal protein operon."
    Zurawski G., Zurawski S.M.
    Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  7. Noorani S.M., Lindahl L., Zengel J.M.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
    Strain: ECOR 30.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "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.
  10. "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.
  11. "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.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS10_ECOLI
AccessioniPrimary (citable) accession number: P0A7R5
Secondary accession number(s): P02364, Q2M6Y6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 4, 2015
This is version 99 of the entry and version 1 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

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 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.