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P0AGA2

- SECY_ECOLI

UniProt

P0AGA2 - SECY_ECOLI

Protein

Protein translocase subunit SecY

Gene

secY

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. SecY is required to insert newly synthesized SecY into the inner membrane. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true, overexpression also results in FtsH-mediated degradation of SecY.

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. intracellular protein transmembrane transport Source: EcoliWiki
    2. intracellular protein transport Source: EcoliWiki
    3. protein targeting Source: UniProtKB-HAMAP
    4. protein transport by the Sec complex Source: EcoCyc

    Keywords - Biological processi

    Protein transport, Translocation, Transport

    Enzyme and pathway databases

    BioCyciEcoCyc:SECY.
    ECOL316407:JW3262-MONOMER.

    Protein family/group databases

    TCDBi3.A.5.1.1. the general secretory pathway (sec) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein translocase subunit SecY
    Gene namesi
    Name:secY
    Synonyms:prlA
    Ordered Locus Names:b3300, JW3262
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10766. secY.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: EcoliWiki
    2. integral component of plasma membrane Source: EcoCyc
    3. intracellular Source: GOC
    4. plasma membrane Source: EcoliWiki

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi40 – 401P → S in secY100; temperature-sensitive.
    Mutagenesisi60 – 7415Missing: Some loss of viability, supports protein translocation; strongly suppresses defective and missing signal sequences; transient transmembrane channels open. Add
    BLAST
    Mutagenesisi65 – 706Missing: Grows almost as well as wild-type, supports protein translocation; strongly suppresses defective and missing signal sequences; transient transmembrane channels open.
    Mutagenesisi67 – 671F → C in prlA3; altered signal sequence interaction, transient channel opening and closing in presence of oxidant; massive ion flux when cross-linked to SecE C-120 mutation. 1 Publication
    Mutagenesisi167 – 1671G → E in secY100; temperature-sensitive.
    Mutagenesisi240 – 2401G → D in secY24; temperature-sensitive at 42 degrees Celsius, impairs interaction with SecE even at 30 degrees in vitro. 1 Publication
    Mutagenesisi282 – 2821S → R in prlA401; altered signal sequence interaction, transient transmembrane channels open.
    Mutagenesisi286 – 2861F → Y in prlA4-1; altered signal sequence interaction.
    Mutagenesisi287 – 2871P → L in secY161; altered signal sequence interaction.
    Mutagenesisi290 – 2901I → T in secY121; altered signal sequence interaction.
    Mutagenesisi357 – 3571R → H in secY39; cold-sensitive.
    Mutagenesisi363 – 3631A → S in secY40; cold-sensitive.
    Mutagenesisi408 – 4081I → N in prlA4-2; altered signal sequence interaction. 1 Publication
    Mutagenesisi424 – 44320Missing: No longer complements secY24, a temperature-sensitive secY mutation. Add
    BLAST

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 443443Protein translocase subunit SecYPRO_0000131721Add
    BLAST

    Post-translational modificationi

    SecY that is not part of the protein translocation apparatus is degraded by FtsH. Also degraded by FtsH when the SecYEG complex is jammed, or upon treatment with antibiotics that block translation elongation such as chloramphenicol.

    Proteomic databases

    PaxDbiP0AGA2.
    PRIDEiP0AGA2.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AGA2.

    Interactioni

    Subunit structurei

    Component of the Sec protein translocase complex. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. Interacts with SecDF-YajC and YidC; YidC interacts with nascent inner membrane proteins after SecY. SecY probably contacts the 23S rRNA and possibly also ribosomal protein L23 during ribosome docking. A single SecY molecule forms the translocating pore, although interaction with SecA may require oligomers.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    secAP104084EBI-761422,EBI-543213

    Protein-protein interaction databases

    DIPiDIP-59302N.
    IntActiP0AGA2. 2 interactions.
    STRINGi511145.b3300.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AKHelectron microscopy14.90B/Y1-436[»]
    2AKIelectron microscopy14.90B/Y1-436[»]
    3J01electron microscopy-A8-442[»]
    3J45electron microscopy9.50y6-440[»]
    3J46electron microscopy10.10y6-440[»]
    ProteinModelPortaliP0AGA2.
    SMRiP0AGA2. Positions 8-442.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AGA2.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2222CytoplasmicCuratedAdd
    BLAST
    Topological domaini36 – 6025PeriplasmicBy similarityAdd
    BLAST
    Topological domaini97 – 11519CytoplasmicCuratedAdd
    BLAST
    Topological domaini132 – 16433PeriplasmicCuratedAdd
    BLAST
    Topological domaini179 – 1835CytoplasmicCurated
    Topological domaini201 – 22323PeriplasmicCuratedAdd
    BLAST
    Topological domaini238 – 27336CytoplasmicCuratedAdd
    BLAST
    Topological domaini288 – 31326PeriplasmicCuratedAdd
    BLAST
    Topological domaini330 – 38051CytoplasmicCuratedAdd
    BLAST
    Topological domaini396 – 3961PeriplasmicCurated
    Topological domaini414 – 44330CytoplasmicCuratedAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei61 – 7010Helical; Name=Helix 2ACurated
    Intramembranei71 – 766Curated
    Intramembranei77 – 9620Helical; Name=Helix 2BCuratedAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei23 – 3513Helical; Name=1CuratedAdd
    BLAST
    Transmembranei61 – 9636Discontinuously helical; Name=2By similarityAdd
    BLAST
    Transmembranei116 – 13116Helical; Name=3CuratedAdd
    BLAST
    Transmembranei165 – 17814Helical; Name=4CuratedAdd
    BLAST
    Transmembranei184 – 20017Helical; Name=5CuratedAdd
    BLAST
    Transmembranei224 – 23714Helical; Name=6CuratedAdd
    BLAST
    Transmembranei274 – 28714Helical; Name=7CuratedAdd
    BLAST
    Transmembranei314 – 32916Helical; Name=8CuratedAdd
    BLAST
    Transmembranei381 – 39515Helical; Name=9CuratedAdd
    BLAST
    Transmembranei397 – 41317Helical; Name=10CuratedAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SecY/SEC61-alpha family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0201.
    HOGENOMiHOG000080585.
    KOiK03076.
    OMAiAWNVQFY.
    OrthoDBiEOG651SWP.
    PhylomeDBiP0AGA2.

    Family and domain databases

    Gene3Di1.10.3370.10. 1 hit.
    HAMAPiMF_01465. SecY.
    InterProiIPR026593. SecY.
    IPR002208. SecY/SEC61-alpha.
    IPR023201. SecY_su_dom.
    [Graphical view]
    PANTHERiPTHR10906. PTHR10906. 1 hit.
    PfamiPF00344. SecY. 1 hit.
    [Graphical view]
    PIRSFiPIRSF004557. SecY. 1 hit.
    SUPFAMiSSF103491. SSF103491. 1 hit.
    TIGRFAMsiTIGR00967. 3a0501s007. 1 hit.
    PROSITEiPS00755. SECY_1. 1 hit.
    PS00756. SECY_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0AGA2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKQPGLDFQ SAKGGLGELK RRLLFVIGAL IVFRIGSFIP IPGIDAAVLA    50
    KLLEQQRGTI IEMFNMFSGG ALSRASIFAL GIMPYISASI IIQLLTVVHP 100
    TLAEIKKEGE SGRRKISQYT RYGTLVLAIF QSIGIATGLP NMPGMQGLVI 150
    NPGFAFYFTA VVSLVTGTMF LMWLGEQITE RGIGNGISII IFAGIVAGLP 200
    PAIAHTIEQA RQGDLHFLVL LLVAVLVFAV TFFVVFVERG QRRIVVNYAK 250
    RQQGRRVYAA QSTHLPLKVN MAGVIPAIFA SSIILFPATI ASWFGGGTGW 300
    NWLTTISLYL QPGQPLYVLL YASAIIFFCF FYTALVFNPR ETADNLKKSG 350
    AFVPGIRPGE QTAKYIDKVM TRLTLVGALY ITFICLIPEF MRDAMKVPFY 400
    FGGTSLLIVV VVIMDFMAQV QTLMMSSQYE SALKKANLKG YGR 443
    Length:443
    Mass (Da):48,512
    Last modified:July 21, 1986 - v1
    Checksum:i711CA63CD8809763
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01563 Genomic DNA. Translation: CAA25725.1.
    U18997 Genomic DNA. Translation: AAA58097.1.
    U00096 Genomic DNA. Translation: AAC76325.1.
    AP009048 Genomic DNA. Translation: BAE77991.1.
    PIRiA04473. QQECSY.
    RefSeqiNP_417759.1. NC_000913.3.
    YP_492132.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76325; AAC76325; b3300.
    BAE77991; BAE77991; BAE77991.
    GeneIDi12934410.
    947799.
    KEGGiecj:Y75_p3876.
    eco:b3300.
    PATRICi32122032. VBIEscCol129921_3393.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01563 Genomic DNA. Translation: CAA25725.1 .
    U18997 Genomic DNA. Translation: AAA58097.1 .
    U00096 Genomic DNA. Translation: AAC76325.1 .
    AP009048 Genomic DNA. Translation: BAE77991.1 .
    PIRi A04473. QQECSY.
    RefSeqi NP_417759.1. NC_000913.3.
    YP_492132.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AKH electron microscopy 14.90 B/Y 1-436 [» ]
    2AKI electron microscopy 14.90 B/Y 1-436 [» ]
    3J01 electron microscopy - A 8-442 [» ]
    3J45 electron microscopy 9.50 y 6-440 [» ]
    3J46 electron microscopy 10.10 y 6-440 [» ]
    ProteinModelPortali P0AGA2.
    SMRi P0AGA2. Positions 8-442.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59302N.
    IntActi P0AGA2. 2 interactions.
    STRINGi 511145.b3300.

    Protein family/group databases

    TCDBi 3.A.5.1.1. the general secretory pathway (sec) family.

    Proteomic databases

    PaxDbi P0AGA2.
    PRIDEi P0AGA2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76325 ; AAC76325 ; b3300 .
    BAE77991 ; BAE77991 ; BAE77991 .
    GeneIDi 12934410.
    947799.
    KEGGi ecj:Y75_p3876.
    eco:b3300.
    PATRICi 32122032. VBIEscCol129921_3393.

    Organism-specific databases

    EchoBASEi EB0759.
    EcoGenei EG10766. secY.

    Phylogenomic databases

    eggNOGi COG0201.
    HOGENOMi HOG000080585.
    KOi K03076.
    OMAi AWNVQFY.
    OrthoDBi EOG651SWP.
    PhylomeDBi P0AGA2.

    Enzyme and pathway databases

    BioCyci EcoCyc:SECY.
    ECOL316407:JW3262-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AGA2.
    PROi P0AGA2.

    Gene expression databases

    Genevestigatori P0AGA2.

    Family and domain databases

    Gene3Di 1.10.3370.10. 1 hit.
    HAMAPi MF_01465. SecY.
    InterProi IPR026593. SecY.
    IPR002208. SecY/SEC61-alpha.
    IPR023201. SecY_su_dom.
    [Graphical view ]
    PANTHERi PTHR10906. PTHR10906. 1 hit.
    Pfami PF00344. SecY. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF004557. SecY. 1 hit.
    SUPFAMi SSF103491. SSF103491. 1 hit.
    TIGRFAMsi TIGR00967. 3a0501s007. 1 hit.
    PROSITEi PS00755. SECY_1. 1 hit.
    PS00756. SECY_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    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. "Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli."
      Akiyama Y., Ito K.
      EMBO J. 6:3465-3470(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.
    5. "Temperature-sensitive sec mutants of Escherichia coli: inhibition of protein export at the permissive temperature."
      Ito K., Hirota Y., Akiyama Y.
      J. Bacteriol. 171:1742-1743(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTANT SECY100.
    6. "Export of Escherichia coli alkaline phosphatase attached to an integral membrane protein, SecY."
      Akiyama Y., Ito K.
      J. Biol. Chem. 264:437-442(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: REQUIRED FOR ITS OWN INSERTION INTO MEMBRANES.
      Strain: K12 / MC4100.
    7. "Characterization of cold-sensitive secY mutants of Escherichia coli."
      Baba T., Jacq A., Brickman E., Beckwith J., Taura T., Ueguchi C., Akiyama Y., Ito K.
      J. Bacteriol. 172:7005-7010(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTANTS SECY39 AND SECY40.
    8. "Novel prlA alleles defective in supporting staphylokinase processing in Escherichia coli."
      Sako T.
      J. Bacteriol. 173:2289-2296(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTANTS SECY121 AND SECY161.
    9. "Biochemical analysis of the biogenesis and function of the Escherichia coli export factor SecY."
      Swidersky U.E., Rienhoefer-Schweer A., Werner P.K., Ernst F., Benson S.A., Hoffschulte H.K., Mueller M.
      Eur. J. Biochem. 207:803-811(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    10. "PrlA suppressor mutations cluster in regions corresponding to three distinct topological domains."
      Osborne R.S., Silhavy T.J.
      EMBO J. 12:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTANTS.
    11. "A cytoplasmic domain is important for the formation of a SecY-SecE translocator complex."
      Baba T., Taura T., Shimoike T., Akiyama Y., Yoshihisa T., Ito K.
      Proc. Natl. Acad. Sci. U.S.A. 91:4539-4543(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-240.
      Strain: K12 / MC4100.
    12. "The allele-specific synthetic lethality of prlA-prlG double mutants predicts interactive domains of SecY and SecE."
      Flower A.M., Osborne R.S., Silhavy T.J.
      EMBO J. 14:884-893(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTANTS.
    13. "FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit."
      Kihara A., Akiyama Y., Ito K.
      Proc. Natl. Acad. Sci. U.S.A. 92:4532-4536(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEGRADATION BY FTSH.
    14. "Sec-dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC."
      Urbanus M.L., Scotti P.A., Froderberg L., Saaf A., de Gier J.W., Brunner J., Samuelson J.C., Dalbey R.E., Oudega B., Luirink J.
      EMBO Rep. 2:524-529(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FTSQ BEFORE YIDC.
    15. "Global topology analysis of the Escherichia coli inner membrane proteome."
      Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
      Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
      Strain: K12 / MG1655 / ATCC 47076.
    16. "Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel."
      Osborne A.R., Rapoport T.A.
      Cell 129:97-110(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SECA, CHARACTERIZATION OF THE TRANSLOCATING PORE.
    17. "Effects of antibiotics and a proto-oncogene homolog on destruction of protein translocator SecY."
      van Stelten J., Silva F., Belin D., Silhavy T.J.
      Science 325:753-756(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPLEX DEGRADATION.
      Strain: K12 / MC4100.
    18. "Determining the conductance of the SecY protein translocation channel for small molecules."
      Saparov S.M., Erlandson K., Cannon K., Schaletzky J., Schulman S., Rapoport T.A., Pohl P.
      Mol. Cell 26:501-509(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF CHANNEL OPENING, MUTAGENESIS OF 60-ILE--ARG-74; 65-ASN--GLY-70; PHE-67 AND ILE-408.
    19. "The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal."
      Li W., Schulman S., Boyd D., Erlandson K., Beckwith J., Rapoport T.A.
      Mol. Cell 26:511-521(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 60-ILE--ARG-74 AND 65-ASN--GLY-70.
    20. "Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes."
      Egea P.F., Stroud R.M.
      Proc. Natl. Acad. Sci. U.S.A. 107:17182-17187(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 424-MET--ARG-443.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    21. "Structure of the E. coli protein-conducting channel bound to a translating ribosome."
      Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., Brooks C.L. III, Ban N., Frank J.
      Nature 438:318-324(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (14.9 ANGSTROMS) OF 1-436 IN COMPLEX WITH THE RIBOSOME AND A NASCENT POLYPEPTIDE CHAIN.
      Strain: MRE-600.
    22. Cited for: STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH THE RIBOSOME AND A NASCENT POLYPEPTIDE CHAIN.
    23. "Structure, function, and biogenesis of SecY, an integral membrane protein involved in protein export."
      Ito K.
      J. Bioenerg. Biomembr. 22:353-367(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    24. "Protein translocation across the bacterial cytoplasmic membrane."
      Driessen A.J., Nouwen N.
      Annu. Rev. Biochem. 77:643-667(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiSECY_ECOLI
    AccessioniPrimary (citable) accession number: P0AGA2
    Secondary accession number(s): P03844, Q2M6W5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 76 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, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3