Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

30S ribosomal protein S2

Gene

rpsB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for ribosomal protein S1 to bind to the 30S subunit.1 Publication

GO - Molecular functioni

  • structural constituent of ribosome Source: GO_Central
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10901-MONOMER.
ECOL316407:JW0164-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S2
Gene namesi
Name:rpsB
Ordered Locus Names:b0169, JW0164
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10901. rpsB.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 24124030S ribosomal protein S2PRO_0000134165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei115 – 1151N6-succinyllysine1 Publication

Proteomic databases

PaxDbiP0A7V0.
PRIDEiP0A7V0.

2D gel databases

SWISS-2DPAGEP0A7V0.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit, contacts S1. Some nascent polypeptide chains are able to cross-link to this protein in situ.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
hslRP0ACG82EBI-543439,EBI-562824

Protein-protein interaction databases

BioGridi852185. 1 interaction.
DIPiDIP-6877N.
IntActiP0A7V0. 206 interactions.
STRINGi511145.b0169.

Structurei

Secondary structure

1
241
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 303Combined sources
Helixi34 – 374Combined sources
Beta strandi38 – 403Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-B6-214[»]
2YKRelectron microscopy9.80B9-226[»]
3J9Yelectron microscopy3.90b1-240[»]
4A2Ielectron microscopy16.50B9-226[»]
4ADVelectron microscopy13.50B2-241[»]
4ODLX-ray2.92C/D/E/F20-34[»]
4ODMX-ray1.75E/F/G/H/I/J/K/L/M20-34[»]
4ODNX-ray1.60B26-41[»]
4ODPX-ray1.75B20-34[»]
4U1UX-ray2.95AB/CB9-226[»]
4U1VX-ray3.00AB/CB9-226[»]
4U20X-ray2.90AB/CB9-226[»]
4U24X-ray2.90AB/CB9-226[»]
4U25X-ray2.90AB/CB9-226[»]
4U26X-ray2.80AB/CB9-226[»]
4U27X-ray2.80AB/CB9-226[»]
4V48electron microscopy11.50BB2-241[»]
4V4HX-ray3.46AB/CB1-241[»]
4V4QX-ray3.46AB/CB2-241[»]
4V4Velectron microscopy15.00AB6-241[»]
4V4Welectron microscopy15.00AB6-241[»]
4V50X-ray3.22AB/CB2-241[»]
4V52X-ray3.21AB/CB2-241[»]
4V53X-ray3.54AB/CB2-241[»]
4V54X-ray3.30AB/CB2-241[»]
4V55X-ray4.00AB/CB2-241[»]
4V56X-ray3.93AB/CB2-241[»]
4V57X-ray3.50AB/CB2-241[»]
4V5BX-ray3.74BB/DB2-241[»]
4V5Helectron microscopy5.80AB9-226[»]
4V5YX-ray4.45AB/CB2-241[»]
4V64X-ray3.50AB/CB2-241[»]
4V65electron microscopy9.00AB1-241[»]
4V66electron microscopy9.00AB1-241[»]
4V69electron microscopy6.70AB9-226[»]
4V6CX-ray3.19AB/CB1-241[»]
4V6DX-ray3.81AB/CB1-241[»]
4V6EX-ray3.71AB/CB1-241[»]
4V6Kelectron microscopy8.25BF1-241[»]
4V6Lelectron microscopy13.20AF1-241[»]
4V6Melectron microscopy7.10AB2-241[»]
4V6Nelectron microscopy12.10BE2-241[»]
4V6Oelectron microscopy14.70AE2-241[»]
4V6Pelectron microscopy13.50AE2-241[»]
4V6Qelectron microscopy11.50AE2-241[»]
4V6Relectron microscopy11.50AE2-241[»]
4V6Selectron microscopy13.10BD2-241[»]
4V6Telectron microscopy8.30AB9-226[»]
4V6Velectron microscopy9.80AB2-241[»]
4V6Yelectron microscopy12.00AB9-226[»]
4V6Zelectron microscopy12.00AB9-226[»]
4V70electron microscopy17.00AB9-226[»]
4V71electron microscopy20.00AB9-226[»]
4V72electron microscopy13.00AB9-226[»]
4V73electron microscopy15.00AB9-226[»]
4V74electron microscopy17.00AB9-226[»]
4V75electron microscopy12.00AB9-226[»]
4V76electron microscopy17.00AB9-226[»]
4V77electron microscopy17.00AB9-226[»]
4V78electron microscopy20.00AB9-226[»]
4V79electron microscopy15.00AB9-226[»]
4V7Aelectron microscopy9.00AB9-226[»]
4V7Belectron microscopy6.80AB1-241[»]
4V7Celectron microscopy7.60AB2-241[»]
4V7Delectron microscopy7.60BB2-241[»]
4V7Ielectron microscopy9.60BB1-241[»]
4V7SX-ray3.25AB/CB9-226[»]
4V7TX-ray3.19AB/CB9-226[»]
4V7UX-ray3.10AB/CB9-226[»]
4V7VX-ray3.29AB/CB9-226[»]
4V85X-ray3.20B1-241[»]
4V89X-ray3.70AB1-241[»]
4V9CX-ray3.30AB/CB1-241[»]
4V9DX-ray3.00AB/BB9-226[»]
4V9OX-ray2.90BB/DB/FB/HB1-241[»]
4V9PX-ray2.90BB/DB/FB/HB1-241[»]
4WF1X-ray3.09AB/CB9-226[»]
4WWWX-ray3.10QB/XB9-226[»]
4YBBX-ray2.10AB/BB4-227[»]
5AFIelectron microscopy2.90b1-240[»]
ProteinModelPortaliP0A7V0.
SMRiP0A7V0. Positions 9-226.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7V0.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S2P family.Curated

Phylogenomic databases

eggNOGiCOG0052.
HOGENOMiHOG000071892.
InParanoidiP0A7V0.
KOiK02967.
OMAiRIPDILY.
OrthoDBiEOG6XWV6P.
PhylomeDBiP0A7V0.

Family and domain databases

HAMAPiMF_00291_B. Ribosomal_S2_B.
InterProiIPR001865. Ribosomal_S2.
IPR005706. Ribosomal_S2_bac/mit/plastid.
IPR018130. Ribosomal_S2_CS.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR12534. PTHR12534. 1 hit.
PfamiPF00318. Ribosomal_S2. 1 hit.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01011. rpsB_bact. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7V0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVSMRDML KAGVHFGHQT RYWNPKMKPF IFGARNKVHI INLEKTVPMF
60 70 80 90 100
NEALAELNKI ASRKGKILFV GTKRAASEAV KDAALSCDQF FVNHRWLGGM
110 120 130 140 150
LTNWKTVRQS IKRLKDLETQ SQDGTFDKLT KKEALMRTRE LEKLENSLGG
160 170 180 190 200
IKDMGGLPDA LFVIDADHEH IAIKEANNLG IPVFAIVDTN SDPDGVDFVI
210 220 230 240
PGNDDAIRAV TLYLGAVAAT VREGRSQDLA SQAEESFVEA E
Length:241
Mass (Da):26,744
Last modified:January 23, 2007 - v2
Checksum:i87A38C696115212E
GO

Mass spectrometryi

Molecular mass is 26610.5 Da from positions 2 - 241. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00343 Genomic DNA. Translation: CAA23631.1.
U70214 Genomic DNA. Translation: AAB08598.1.
U00096 Genomic DNA. Translation: AAC73280.1.
AP009048 Genomic DNA. Translation: BAB96744.1.
PIRiA02696. R3EC2.
RefSeqiNP_414711.1. NC_000913.3.
WP_000246882.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC73280; AAC73280; b0169.
BAB96744; BAB96744; BAB96744.
GeneIDi947874.
KEGGieco:b0169.
PATRICi32115445. VBIEscCol129921_0174.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00343 Genomic DNA. Translation: CAA23631.1.
U70214 Genomic DNA. Translation: AAB08598.1.
U00096 Genomic DNA. Translation: AAC73280.1.
AP009048 Genomic DNA. Translation: BAB96744.1.
PIRiA02696. R3EC2.
RefSeqiNP_414711.1. NC_000913.3.
WP_000246882.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-B6-214[»]
2YKRelectron microscopy9.80B9-226[»]
3J9Yelectron microscopy3.90b1-240[»]
4A2Ielectron microscopy16.50B9-226[»]
4ADVelectron microscopy13.50B2-241[»]
4ODLX-ray2.92C/D/E/F20-34[»]
4ODMX-ray1.75E/F/G/H/I/J/K/L/M20-34[»]
4ODNX-ray1.60B26-41[»]
4ODPX-ray1.75B20-34[»]
4U1UX-ray2.95AB/CB9-226[»]
4U1VX-ray3.00AB/CB9-226[»]
4U20X-ray2.90AB/CB9-226[»]
4U24X-ray2.90AB/CB9-226[»]
4U25X-ray2.90AB/CB9-226[»]
4U26X-ray2.80AB/CB9-226[»]
4U27X-ray2.80AB/CB9-226[»]
4V48electron microscopy11.50BB2-241[»]
4V4HX-ray3.46AB/CB1-241[»]
4V4QX-ray3.46AB/CB2-241[»]
4V4Velectron microscopy15.00AB6-241[»]
4V4Welectron microscopy15.00AB6-241[»]
4V50X-ray3.22AB/CB2-241[»]
4V52X-ray3.21AB/CB2-241[»]
4V53X-ray3.54AB/CB2-241[»]
4V54X-ray3.30AB/CB2-241[»]
4V55X-ray4.00AB/CB2-241[»]
4V56X-ray3.93AB/CB2-241[»]
4V57X-ray3.50AB/CB2-241[»]
4V5BX-ray3.74BB/DB2-241[»]
4V5Helectron microscopy5.80AB9-226[»]
4V5YX-ray4.45AB/CB2-241[»]
4V64X-ray3.50AB/CB2-241[»]
4V65electron microscopy9.00AB1-241[»]
4V66electron microscopy9.00AB1-241[»]
4V69electron microscopy6.70AB9-226[»]
4V6CX-ray3.19AB/CB1-241[»]
4V6DX-ray3.81AB/CB1-241[»]
4V6EX-ray3.71AB/CB1-241[»]
4V6Kelectron microscopy8.25BF1-241[»]
4V6Lelectron microscopy13.20AF1-241[»]
4V6Melectron microscopy7.10AB2-241[»]
4V6Nelectron microscopy12.10BE2-241[»]
4V6Oelectron microscopy14.70AE2-241[»]
4V6Pelectron microscopy13.50AE2-241[»]
4V6Qelectron microscopy11.50AE2-241[»]
4V6Relectron microscopy11.50AE2-241[»]
4V6Selectron microscopy13.10BD2-241[»]
4V6Telectron microscopy8.30AB9-226[»]
4V6Velectron microscopy9.80AB2-241[»]
4V6Yelectron microscopy12.00AB9-226[»]
4V6Zelectron microscopy12.00AB9-226[»]
4V70electron microscopy17.00AB9-226[»]
4V71electron microscopy20.00AB9-226[»]
4V72electron microscopy13.00AB9-226[»]
4V73electron microscopy15.00AB9-226[»]
4V74electron microscopy17.00AB9-226[»]
4V75electron microscopy12.00AB9-226[»]
4V76electron microscopy17.00AB9-226[»]
4V77electron microscopy17.00AB9-226[»]
4V78electron microscopy20.00AB9-226[»]
4V79electron microscopy15.00AB9-226[»]
4V7Aelectron microscopy9.00AB9-226[»]
4V7Belectron microscopy6.80AB1-241[»]
4V7Celectron microscopy7.60AB2-241[»]
4V7Delectron microscopy7.60BB2-241[»]
4V7Ielectron microscopy9.60BB1-241[»]
4V7SX-ray3.25AB/CB9-226[»]
4V7TX-ray3.19AB/CB9-226[»]
4V7UX-ray3.10AB/CB9-226[»]
4V7VX-ray3.29AB/CB9-226[»]
4V85X-ray3.20B1-241[»]
4V89X-ray3.70AB1-241[»]
4V9CX-ray3.30AB/CB1-241[»]
4V9DX-ray3.00AB/BB9-226[»]
4V9OX-ray2.90BB/DB/FB/HB1-241[»]
4V9PX-ray2.90BB/DB/FB/HB1-241[»]
4WF1X-ray3.09AB/CB9-226[»]
4WWWX-ray3.10QB/XB9-226[»]
4YBBX-ray2.10AB/BB4-227[»]
5AFIelectron microscopy2.90b1-240[»]
ProteinModelPortaliP0A7V0.
SMRiP0A7V0. Positions 9-226.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852185. 1 interaction.
DIPiDIP-6877N.
IntActiP0A7V0. 206 interactions.
STRINGi511145.b0169.

Chemistry

ChEMBLiCHEMBL2363135.

2D gel databases

SWISS-2DPAGEP0A7V0.

Proteomic databases

PaxDbiP0A7V0.
PRIDEiP0A7V0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73280; AAC73280; b0169.
BAB96744; BAB96744; BAB96744.
GeneIDi947874.
KEGGieco:b0169.
PATRICi32115445. VBIEscCol129921_0174.

Organism-specific databases

EchoBASEiEB0894.
EcoGeneiEG10901. rpsB.

Phylogenomic databases

eggNOGiCOG0052.
HOGENOMiHOG000071892.
InParanoidiP0A7V0.
KOiK02967.
OMAiRIPDILY.
OrthoDBiEOG6XWV6P.
PhylomeDBiP0A7V0.

Enzyme and pathway databases

BioCyciEcoCyc:EG10901-MONOMER.
ECOL316407:JW0164-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7V0.
PROiP0A7V0.

Family and domain databases

HAMAPiMF_00291_B. Ribosomal_S2_B.
InterProiIPR001865. Ribosomal_S2.
IPR005706. Ribosomal_S2_bac/mit/plastid.
IPR018130. Ribosomal_S2_CS.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR12534. PTHR12534. 1 hit.
PfamiPF00318. Ribosomal_S2. 1 hit.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01011. rpsB_bact. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Organization and nucleotide sequence of a new ribosomal operon in Escherichia coli containing the genes for ribosomal protein S2 and elongation factor Ts."
    An G., Bendiak D.S., Mamelak L.A., Friesen J.D.
    Nucleic Acids Res. 9:4163-4172(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
    Fujita N., Mori H., Yura T., Ishihama A.
    Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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. "Primary structure of protein S2 from the Escherichia coli ribosome."
    Wittmann-Liebold B., Bosserhoff A.
    FEBS Lett. 129:10-16(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-241.
    Strain: K12.
  7. "Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit."
    Ueshima R., Fujita N., Ishihama A.
    Biochem. Biophys. Res. Commun. 184:634-639(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-31.
  8. "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 2-13.
    Strain: K12 / EMG2.
  9. "Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
    Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
    EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-35, CROSS-LINKING TO RRNA.
    Strain: MRE-600.
  10. "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.
  11. "Flexibility of the nascent polypeptide chain within the ribosome --contacts from the peptide N-terminus to a specific region of the 30S subunit."
    Choi K.M., Atkins J.F., Gesteland R.F., Brimacombe R.
    Eur. J. Biochem. 255:409-413(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO NASCENT POLYPEPTIDE CHAINS.
  12. "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.
  13. "Effects of ribosomal proteins S1, S2 and the DeaD/CsdA DEAD-box helicase on translation of leaderless and canonical mRNAs in Escherichia coli."
    Moll I., Grill S., Gruendling A., Blaesi U.
    Mol. Microbiol. 44:1387-1396(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  14. "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.
  15. "Identification of lysine succinylation as a new post-translational modification."
    Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
    Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION AT LYS-115.
    Strain: K12.
  16. "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), SUBUNIT.
    Strain: MRE-600.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES, SUBUNIT.
    Strain: MRE-600.

Entry informationi

Entry nameiRS2_ECOLI
AccessioniPrimary (citable) accession number: P0A7V0
Secondary accession number(s): P02351, Q9R2E5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 113 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

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.