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Protein

Cysteine desulfurase IscS

Gene

iscS

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

Functioni

Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Preferentially binds to disordered IscU on which the Fe-S is assembled, IscU converts to the structured state and then dissociates from IscS to transfer the Fe-S to an acceptor protein. Also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate. Transfers sulfur onto 'Cys-456' of ThiI and onto 'Cys-19' of TusA in transpersulfidation reactions.10 Publications

Catalytic activityi

L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.UniRule annotation1 Publication

Cofactori

pyridoxal 5'-phosphateUniRule annotation2 Publications

Enzyme regulationi

Treatment with N-ethylmaleimide inhibits sulfur transfer. Activated by ThiI and TusA.3 Publications

Kineticsi

kcat is 8.5 min(-1).1 Publication

  1. KM=2.7 µM for L-cysteine1 Publication

    Pathwayi: iron-sulfur cluster biosynthesis

    This protein is involved in the pathway iron-sulfur cluster biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation1 Publication
    View all proteins of this organism that are known to be involved in the pathway iron-sulfur cluster biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei155 – 1551Pyridoxal phosphateUniRule annotation
    Binding sitei183 – 1831Pyridoxal phosphateUniRule annotation1 Publication
    Binding sitei243 – 2431Pyridoxal phosphateUniRule annotation1 Publication
    Active sitei328 – 3281Cysteine persulfide intermediateUniRule annotation2 Publications
    Metal bindingi328 – 3281Iron-sulfur (2Fe-2S); via persulfide group; shared with IscUUniRule annotation

    GO - Molecular functioni

    • 2 iron, 2 sulfur cluster binding Source: UniProtKB-HAMAP
    • cysteine desulfurase activity Source: EcoCyc
    • metal ion binding Source: UniProtKB-KW
    • pyridoxal phosphate binding Source: EcoCyc
    • selenocysteine lyase activity Source: EcoCyc
    • sulfur carrier activity Source: EcoCyc

    GO - Biological processi

    • [2Fe-2S] cluster assembly Source: UniProtKB-HAMAP
    • iron-sulfur cluster assembly Source: EcoCyc
    • oxazole or thiazole biosynthetic process Source: EcoCyc
    • tRNA pseudouridine synthesis Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    tRNA processing

    Keywords - Ligandi

    2Fe-2S, Iron, Iron-sulfur, Metal-binding, Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:G7325-MONOMER.
    ECOL316407:JW2514-MONOMER.
    MetaCyc:G7325-MONOMER.
    UniPathwayiUPA00266.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cysteine desulfurase IscS1 PublicationUniRule annotation (EC:2.8.1.7UniRule annotation1 Publication)
    Alternative name(s):
    NifS protein homolog1 Publication
    ThiI transpersulfidase1 Publication
    TusA transpersulfidase1 Publication
    Gene namesi
    Name:iscSUniRule annotation
    Synonyms:nuvC, yfhO, yzzO
    Ordered Locus Names:b2530, JW2514
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG12677. iscS.

    Subcellular locationi

    • Cytoplasm UniRule annotationCurated

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene lose sulfurtransferase activity and require thiamine and nicotinic acid for growth. Under aerobic conditions the deletion of IscS causes an auxotrophy for thiamine and nicotinic acid, whereas under anaerobic conditions, only nicotinic acid s required.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi328 – 3281C → A: Loss of cysteine desulfurization. 1 Publication
    Mutagenesisi376 – 40429Missing : Normal cysteine desulfurase activity, decreased binding to IscU, decreased sulfur transfer to IscU, decreased Fe-S cluster assembly. 1 PublicationAdd
    BLAST

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 404404Cysteine desulfurase IscSPRO_0000150264Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei206 – 2061N6-(pyridoxal phosphate)lysineUniRule annotation1 Publication

    Proteomic databases

    EPDiP0A6B7.
    PaxDbiP0A6B7.
    PRIDEiP0A6B7.

    Interactioni

    Subunit structurei

    Homodimer. The homodimer interacts with IscU and TusA, other S acceptors. Each subunit of the IscS dimer contacts a IscU monomer.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    iscUP0ACD48EBI-550055,EBI-561646
    rhdAP521972EBI-550055,EBI-7906952From a different organism.
    tusAP0A8905EBI-550055,EBI-561780

    Protein-protein interaction databases

    BioGridi4263511. 524 interactions.
    DIPiDIP-29109N.
    IntActiP0A6B7. 45 interactions.
    MINTiMINT-236550.
    STRINGi511145.b2530.

    Structurei

    Secondary structure

    1
    404
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63Combined sources
    Turni9 – 113Combined sources
    Helixi17 – 237Combined sources
    Helixi24 – 263Combined sources
    Helixi42 – 6221Combined sources
    Helixi66 – 683Combined sources
    Beta strandi69 – 735Combined sources
    Helixi75 – 9016Combined sources
    Helixi91 – 933Combined sources
    Beta strandi96 – 1005Combined sources
    Helixi105 – 11612Combined sources
    Beta strandi120 – 1245Combined sources
    Helixi134 – 1407Combined sources
    Beta strandi145 – 1495Combined sources
    Turni155 – 1573Combined sources
    Helixi163 – 17311Combined sources
    Beta strandi176 – 1805Combined sources
    Turni182 – 1876Combined sources
    Turni192 – 1943Combined sources
    Beta strandi198 – 2047Combined sources
    Turni205 – 2084Combined sources
    Beta strandi214 – 2185Combined sources
    Turni220 – 2234Combined sources
    Turni235 – 2395Combined sources
    Helixi246 – 27934Combined sources
    Turni280 – 2834Combined sources
    Beta strandi287 – 2915Combined sources
    Turni293 – 2953Combined sources
    Beta strandi300 – 3056Combined sources
    Helixi310 – 3167Combined sources
    Turni317 – 3193Combined sources
    Helixi337 – 3426Combined sources
    Helixi346 – 3505Combined sources
    Beta strandi352 – 3565Combined sources
    Helixi363 – 38220Combined sources
    Helixi385 – 3906Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P3WX-ray2.10A/B1-404[»]
    ProteinModelPortaliP0A6B7.
    SMRiP0A6B7. Positions 1-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A6B7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni75 – 762Pyridoxal phosphate bindingUniRule annotation
    Regioni203 – 2053Pyridoxal phosphate bindingUniRule annotation1 Publication

    Domaini

    The C-terminus (residues 376-404) is important for interaction with IscU.1 Publication

    Sequence similaritiesi

    Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105C3J. Bacteria.
    COG1104. LUCA.
    HOGENOMiHOG000017510.
    InParanoidiP0A6B7.
    KOiK04487.
    OMAiEPIQSGG.
    OrthoDBiEOG62RSBK.
    PhylomeDBiP0A6B7.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_00331. Cys_desulf_IscS.
    InterProiIPR000192. Aminotrans_V_dom.
    IPR020578. Aminotrans_V_PyrdxlP_BS.
    IPR010240. Cys_deSase_IscS.
    IPR016454. Cysteine_dSase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00266. Aminotran_5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005572. NifS. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR02006. IscS. 1 hit.
    PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A6B7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKLPIYLDYS ATTPVDPRVA EKMMQFMTMD GTFGNPASRS HRFGWQAEEA
    60 70 80 90 100
    VDIARNQIAD LVGADPREIV FTSGATESDN LAIKGAANFY QKKGKHIITS
    110 120 130 140 150
    KTEHKAVLDT CRQLEREGFE VTYLAPQRNG IIDLKELEAA MRDDTILVSI
    160 170 180 190 200
    MHVNNEIGVV QDIAAIGEMC RARGIIYHVD ATQSVGKLPI DLSQLKVDLM
    210 220 230 240 250
    SFSGHKIYGP KGIGALYVRR KPRVRIEAQM HGGGHERGMR SGTLPVHQIV
    260 270 280 290 300
    GMGEAYRIAK EEMATEMERL RGLRNRLWNG IKDIEEVYLN GDLEHGAPNI
    310 320 330 340 350
    LNVSFNYVEG ESLIMALKDL AVSSGSACTS ASLEPSYVLR ALGLNDELAH
    360 370 380 390 400
    SSIRFSLGRF TTEEEIDYTI ELVRKSIGRL RDLSPLWEMY KQGVDLNSIE

    WAHH
    Length:404
    Mass (Da):45,090
    Last modified:June 7, 2005 - v1
    Checksum:i1E4F2E6F9CD266B0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311G → D AA sequence (PubMed:8663056).Curated
    Sequence conflicti34 – 341G → F AA sequence (PubMed:8663056).Curated
    Sequence conflicti37 – 382AS → NA AA sequence (PubMed:8663056).Curated
    Sequence conflicti118 – 1181G → L AA sequence (PubMed:8663056).Curated
    Sequence conflicti126 – 1261P → M AA sequence (PubMed:8663056).Curated
    Sequence conflicti320 – 3201L → I AA sequence (PubMed:8663056).Curated
    Sequence conflicti326 – 3272SA → YL AA sequence (PubMed:8663056).Curated
    Sequence conflicti339 – 3391L → V AA sequence (PubMed:8663056).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAT48142.1.
    AP009048 Genomic DNA. Translation: BAA16424.1.
    RefSeqiWP_001295373.1. NZ_LN832404.1.
    YP_026169.1. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAT48142; AAT48142; b2530.
    BAA16424; BAA16424; BAA16424.
    GeneIDi947004.
    KEGGiecj:JW2514.
    eco:b2530.
    PATRICi32120457. VBIEscCol129921_2631.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAT48142.1.
    AP009048 Genomic DNA. Translation: BAA16424.1.
    RefSeqiWP_001295373.1. NZ_LN832404.1.
    YP_026169.1. NC_000913.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P3WX-ray2.10A/B1-404[»]
    ProteinModelPortaliP0A6B7.
    SMRiP0A6B7. Positions 1-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4263511. 524 interactions.
    DIPiDIP-29109N.
    IntActiP0A6B7. 45 interactions.
    MINTiMINT-236550.
    STRINGi511145.b2530.

    Proteomic databases

    EPDiP0A6B7.
    PaxDbiP0A6B7.
    PRIDEiP0A6B7.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAT48142; AAT48142; b2530.
    BAA16424; BAA16424; BAA16424.
    GeneIDi947004.
    KEGGiecj:JW2514.
    eco:b2530.
    PATRICi32120457. VBIEscCol129921_2631.

    Organism-specific databases

    EchoBASEiEB2542.
    EcoGeneiEG12677. iscS.

    Phylogenomic databases

    eggNOGiENOG4105C3J. Bacteria.
    COG1104. LUCA.
    HOGENOMiHOG000017510.
    InParanoidiP0A6B7.
    KOiK04487.
    OMAiEPIQSGG.
    OrthoDBiEOG62RSBK.
    PhylomeDBiP0A6B7.

    Enzyme and pathway databases

    UniPathwayiUPA00266.
    BioCyciEcoCyc:G7325-MONOMER.
    ECOL316407:JW2514-MONOMER.
    MetaCyc:G7325-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP0A6B7.
    PROiP0A6B7.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_00331. Cys_desulf_IscS.
    InterProiIPR000192. Aminotrans_V_dom.
    IPR020578. Aminotrans_V_PyrdxlP_BS.
    IPR010240. Cys_deSase_IscS.
    IPR016454. Cysteine_dSase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00266. Aminotran_5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005572. NifS. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR02006. IscS. 1 hit.
    PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase."
      Flint D.H.
      J. Biol. Chem. 271:16068-16074(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-38; 43-66; 117-127; 212-219; 241-257; 319-339 AND 382-391, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE.
    5. "IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA."
      Kambampati R., Lauhon C.T.
      Biochemistry 38:16561-16568(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-16, FUNCTION, COFACTOR, ENZYME REGULATION.
      Strain: K12.
    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. "Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions."
      Mihara H., Kurihara T., Yoshimura T., Esaki N.
      J. Biochem. 127:559-567(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-9, MUTAGENESIS OF CYS-328.
      Strain: K12.
    8. "Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli."
      Takahashi Y., Nakamura M.
      J. Biochem. 126:917-926(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PATHWAY.
      Strain: C41(DE3).
    9. "Contribution of cysteine desulfurase (NifS protein) to the biotin synthase reaction of Escherichia coli."
      Kiyasu T., Asakura A., Nagahashi Y., Hoshino T.
      J. Bacteriol. 182:2879-2885(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: ATCC 33694 / HB101.
    10. "The iscS gene in Escherichia coli is required for the biosynthesis of 4-thiouridine, thiamine, and NAD."
      Lauhon C.T., Kambampati R.
      J. Biol. Chem. 275:20096-20103(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
      Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
    11. "Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate."
      Lacourciere G.M., Mihara H., Kurihara T., Esaki N., Stadtman T.C.
      J. Biol. Chem. 275:23769-23773(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SELENIUM DELIVERY.
      Strain: MBO8.
    12. "The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli."
      Schwartz C.J., Djaman O., Imlay J.A., Kiley P.J.
      Proc. Natl. Acad. Sci. U.S.A. 97:9009-9014(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
      Strain: K12 / MG1655 / ATCC 47076.
    13. "Transfer of sulfur from IscS to IscU during Fe/S cluster assembly."
      Urbina H.D., Silberg J.J., Hoff K.G., Vickery L.E.
      J. Biol. Chem. 276:44521-44526(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SULFUR TRANSFER, INTERACTION WITH ISCU, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, MUTAGENESIS OF 376-SER--HIS-404.
      Strain: K12.
    14. "Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions."
      Ikeuchi Y., Shigi N., Kato J., Nishimura A., Suzuki T.
      Mol. Cell 21:97-108(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, ENZYME REGULATION.
    15. "Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase."
      Kim J.H., Tonelli M., Markley J.L.
      Proc. Natl. Acad. Sci. U.S.A. 109:454-459(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    16. "Crystal structure of IscS, a cysteine desulfurase from Escherichia coli."
      Cupp-Vickery J.R., Urbina H., Vickery L.E.
      J. Mol. Biol. 330:1049-1059(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, PYRIDOXAL PHOSPHATE AT LYS-206, COFACTOR, SUBUNIT, ACTIVE SITE.

    Entry informationi

    Entry nameiISCS_ECOLI
    AccessioniPrimary (citable) accession number: P0A6B7
    Secondary accession number(s): P39171
    , P76581, P76992, Q8XA86
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: July 6, 2016
    This is version 104 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    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.