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P0AGD7

- SRP54_ECOLI

UniProt

P0AGD7 - SRP54_ECOLI

Protein

Signal recognition particle protein

Gene

ffh

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 90 (01 Oct 2014)
      Sequence version 1 (20 Dec 2005)
      Previous versions | rss
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    Functioni

    Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components.7 PublicationsUniRule annotation

    Enzyme regulationi

    Conformation of the Ffh-FtsY complex and regulation of its GTPase activity are modulated by the 4.5S RNA. Formation of the FfH-FtsY complex leads to a mutual stimulation of both GTPases.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi107 – 1148GTPUniRule annotation
    Nucleotide bindingi190 – 1945GTPUniRule annotation
    Nucleotide bindingi248 – 2514GTPUniRule annotation

    GO - Molecular functioni

    1. 7S RNA binding Source: InterPro
    2. GTPase activity Source: EcoCyc
    3. GTP binding Source: EcoliWiki

    GO - Biological processi

    1. GTP catabolic process Source: GOC
    2. protein targeting to membrane Source: EcoliWiki
    3. SRP-dependent cotranslational protein targeting to membrane Source: InterPro

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding, RNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10300-MONOMER.
    ECOL316407:JW5414-MONOMER.

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Signal recognition particle proteinUniRule annotation
    Alternative name(s):
    Fifty-four homologUniRule annotation
    Short name:
    Ffh
    p48
    Gene namesi
    Name:ffhUniRule annotation
    Ordered Locus Names:b2610, JW5414
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10300. ffh.

    Subcellular locationi

    Cytoplasm
    Note: The SRP-RNC complex is targeted to the cytoplasmic membrane.

    GO - Cellular componenti

    1. ribonucleoprotein complex Source: EcoliWiki
    2. signal recognition particle Source: EcoliWiki
    3. signal recognition particle, endoplasmic reticulum targeting Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Signal recognition particle

    Pathology & Biotechi

    Disruption phenotypei

    Essential; deletion experiments lead to loss of inner membrane protein targeting. Also leads to reduced targeting of lipoproteins Lpp and BRP.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 453453Signal recognition particle proteinPRO_0000101153Add
    BLAST

    Proteomic databases

    PaxDbiP0AGD7.
    PRIDEiP0AGD7.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AGD7.

    Interactioni

    Subunit structurei

    Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY. SRP is a ribonucleoprotein composed of Ffh and a 4.5S RNA molecule. Metal ions are essential for the formation and stability of the SRP complex. Interacts with the ribosomes, via ribosomal protein L23. Interacts with FtsY.7 PublicationsUniRule annotation

    Protein-protein interaction databases

    DIPiDIP-31865N.
    IntActiP0AGD7. 19 interactions.
    MINTiMINT-1218614.
    STRINGi511145.b2610.

    Structurei

    Secondary structure

    1
    453
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 1511
    Helixi24 – 4017
    Helixi45 – 6016
    Helixi70 – 8617
    Beta strandi96 – 10611
    Helixi113 – 12614
    Beta strandi132 – 1365
    Helixi144 – 15512
    Beta strandi158 – 1603
    Helixi168 – 18114
    Beta strandi185 – 1906
    Helixi199 – 21214
    Beta strandi215 – 2228
    Helixi229 – 23911
    Beta strandi244 – 2485
    Helixi258 – 2669
    Beta strandi270 – 2745
    Beta strandi276 – 2783
    Beta strandi282 – 2843
    Helixi287 – 2959
    Helixi331 – 3388
    Helixi373 – 3819
    Helixi385 – 3895
    Helixi391 – 3933
    Helixi396 – 40510
    Helixi410 – 43021

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DULX-ray1.80A329-430[»]
    1HQ1X-ray1.52A328-432[»]
    2J28electron microscopy8.0092-431[»]
    2PXBX-ray2.00A329-430[»]
    2PXDX-ray2.00A329-430[»]
    2PXEX-ray2.00A329-430[»]
    2PXFX-ray2.00A329-430[»]
    2PXKX-ray2.00A329-430[»]
    2PXLX-ray2.50A329-430[»]
    2PXPX-ray2.50A329-430[»]
    2PXQX-ray2.50A329-430[»]
    2PXTX-ray2.50A329-430[»]
    2PXUX-ray2.50A329-430[»]
    2PXVX-ray2.00A329-430[»]
    2XKVelectron microscopy13.50C329-430[»]
    2XXAX-ray3.94A/C1-433[»]
    3LQXX-ray1.93A329-428[»]
    4C7OX-ray2.60A/C1-298[»]
    ProteinModelPortaliP0AGD7.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AGD7.

    Family & Domainsi

    Domaini

    Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC.2 PublicationsUniRule annotation

    Sequence similaritiesi

    Belongs to the GTP-binding SRP family. SRP54 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0541.
    HOGENOMiHOG000036164.
    KOiK03106.
    OMAiLKQHKQM.
    OrthoDBiEOG62K1ZH.
    PhylomeDBiP0AGD7.

    Family and domain databases

    Gene3Di1.10.260.30. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_00306. SRP54.
    InterProiIPR003593. AAA+_ATPase.
    IPR027417. P-loop_NTPase.
    IPR013822. Signal_recog_particl_SRP54_hlx.
    IPR004125. Signal_recog_particle_SRP54_M.
    IPR022941. SRP54.
    IPR000897. SRP54_GTPase_dom.
    IPR004780. SRP_Ffh.
    [Graphical view]
    PANTHERiPTHR11564:SF7. PTHR11564:SF7. 1 hit.
    PfamiPF00448. SRP54. 1 hit.
    PF02881. SRP54_N. 1 hit.
    PF02978. SRP_SPB. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM00962. SRP54. 1 hit.
    SM00963. SRP54_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47446. SSF47446. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00959. ffh. 1 hit.
    PROSITEiPS00300. SRP54. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0AGD7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFDNLTDRLS RTLRNISGRG RLTEDNVKDT LREVRMALLE ADVALPVVRE    50
    FINRVKEKAV GHEVNKSLTP GQEFVKIVRN ELVAAMGEEN QTLNLAAQPP 100
    AVVLMAGLQG AGKTTSVGKL GKFLREKHKK KVLVVSADVY RPAAIKQLET 150
    LAEQVGVDFF PSDVGQKPVD IVNAALKEAK LKFYDVLLVD TAGRLHVDEA 200
    MMDEIKQVHA SINPVETLFV VDAMTGQDAA NTAKAFNEAL PLTGVVLTKV 250
    DGDARGGAAL SIRHITGKPI KFLGVGEKTE ALEPFHPDRI ASRILGMGDV 300
    LSLIEDIESK VDRAQAEKLA SKLKKGDGFD LNDFLEQLRQ MKNMGGMASL 350
    MGKLPGMGQI PDNVKSQMDD KVLVRMEAII NSMTMKERAK PEIIKGSRKR 400
    RIAAGCGMQV QDVNRLLKQF DDMQRMMKKM KKGGMAKMMR SMKGMMPPGF 450
    PGR 453
    Length:453
    Mass (Da):49,787
    Last modified:December 20, 2005 - v1
    Checksum:iE9C7A7101CC04D66
    GO

    Sequence cautioni

    The sequence CAA25957.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01818 Genomic DNA. Translation: CAA25957.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC75659.1.
    AP009048 Genomic DNA. Translation: BAA16495.2.
    PIRiE65039.
    RefSeqiNP_417101.1. NC_000913.3.
    YP_490833.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75659; AAC75659; b2610.
    BAA16495; BAA16495; BAA16495.
    GeneIDi12933092.
    947102.
    KEGGiecj:Y75_p2558.
    eco:b2610.
    PATRICi32120619. VBIEscCol129921_2708.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01818 Genomic DNA. Translation: CAA25957.1 . Different initiation.
    U00096 Genomic DNA. Translation: AAC75659.1 .
    AP009048 Genomic DNA. Translation: BAA16495.2 .
    PIRi E65039.
    RefSeqi NP_417101.1. NC_000913.3.
    YP_490833.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DUL X-ray 1.80 A 329-430 [» ]
    1HQ1 X-ray 1.52 A 328-432 [» ]
    2J28 electron microscopy 8.00 9 2-431 [» ]
    2PXB X-ray 2.00 A 329-430 [» ]
    2PXD X-ray 2.00 A 329-430 [» ]
    2PXE X-ray 2.00 A 329-430 [» ]
    2PXF X-ray 2.00 A 329-430 [» ]
    2PXK X-ray 2.00 A 329-430 [» ]
    2PXL X-ray 2.50 A 329-430 [» ]
    2PXP X-ray 2.50 A 329-430 [» ]
    2PXQ X-ray 2.50 A 329-430 [» ]
    2PXT X-ray 2.50 A 329-430 [» ]
    2PXU X-ray 2.50 A 329-430 [» ]
    2PXV X-ray 2.00 A 329-430 [» ]
    2XKV electron microscopy 13.50 C 329-430 [» ]
    2XXA X-ray 3.94 A/C 1-433 [» ]
    3LQX X-ray 1.93 A 329-428 [» ]
    4C7O X-ray 2.60 A/C 1-298 [» ]
    ProteinModelPortali P0AGD7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-31865N.
    IntActi P0AGD7. 19 interactions.
    MINTi MINT-1218614.
    STRINGi 511145.b2610.

    Protein family/group databases

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

    Proteomic databases

    PaxDbi P0AGD7.
    PRIDEi P0AGD7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75659 ; AAC75659 ; b2610 .
    BAA16495 ; BAA16495 ; BAA16495 .
    GeneIDi 12933092.
    947102.
    KEGGi ecj:Y75_p2558.
    eco:b2610.
    PATRICi 32120619. VBIEscCol129921_2708.

    Organism-specific databases

    EchoBASEi EB0296.
    EcoGenei EG10300. ffh.

    Phylogenomic databases

    eggNOGi COG0541.
    HOGENOMi HOG000036164.
    KOi K03106.
    OMAi LKQHKQM.
    OrthoDBi EOG62K1ZH.
    PhylomeDBi P0AGD7.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10300-MONOMER.
    ECOL316407:JW5414-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AGD7.
    PROi P0AGD7.

    Gene expression databases

    Genevestigatori P0AGD7.

    Family and domain databases

    Gene3Di 1.10.260.30. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPi MF_00306. SRP54.
    InterProi IPR003593. AAA+_ATPase.
    IPR027417. P-loop_NTPase.
    IPR013822. Signal_recog_particl_SRP54_hlx.
    IPR004125. Signal_recog_particle_SRP54_M.
    IPR022941. SRP54.
    IPR000897. SRP54_GTPase_dom.
    IPR004780. SRP_Ffh.
    [Graphical view ]
    PANTHERi PTHR11564:SF7. PTHR11564:SF7. 1 hit.
    Pfami PF00448. SRP54. 1 hit.
    PF02881. SRP54_N. 1 hit.
    PF02978. SRP_SPB. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    SM00962. SRP54. 1 hit.
    SM00963. SRP54_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47446. SSF47446. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00959. ffh. 1 hit.
    PROSITEi PS00300. SRP54. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of an Escherichia coli operon containing genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a 21-K polypeptide."
      Bystroem A.S., Hjalmarsson K.J., Wikstroem P.M., Bjoerk G.R.
      EMBO J. 2:899-905(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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.
    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], SEQUENCE REVISION.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "E. coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle."
      Ribes V., Roemisch K., Giner A., Dobberstein B., Tollervey D.
      Cell 63:591-600(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex."
      Luirink J., High S., Wood H., Giner A., Tollervey D., Dobberstein B.
      Nature 359:741-743(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    7. "The E. coli ffh gene is necessary for viability and efficient protein export."
      Phillips G.J., Silhavy T.J.
      Nature 359:744-746(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    8. "Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor."
      Powers T., Walter P.
      EMBO J. 16:4880-4886(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    9. "Role of SRP RNA in the GTPase cycles of Ffh and FtsY."
      Peluso P., Shan S.O., Nock S., Herschlag D., Walter P.
      Biochemistry 40:15224-15233(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, GTPASE ACTIVITY, ENZYME REGULATION.
    10. "Genetic screen yields mutations in genes encoding all known components of the Escherichia coli signal recognition particle pathway."
      Tian H., Beckwith J.
      J. Bacteriol. 184:111-118(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
      Strain: K12.
    11. "Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome."
      Ullers R.S., Houben E.N.G., Raine A., ten Hagen-Jongman C.M., Ehrenberg M., Brunner J., Oudega B., Harms N., Luirink J.
      J. Cell Biol. 161:679-684(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RIBOSOMAL PROTEIN L23 AND NASCENT PROTEIN CHAINS.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    12. "The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome."
      Gu S.-Q., Peske F., Wieden H.-J., Rodnina M.V., Wintermeyer W.
      RNA 9:566-573(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RIBOSOMAL PROTEIN L23, DOMAIN.
      Strain: MRE-600.
    13. "Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway."
      Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W.
      J. Biol. Chem. 279:31026-31032(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN LIPOPROTEIN EXPORT, DISRUPTION PHENOTYPE.
    14. "Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor."
      Buskiewicz I., Deuerling E., Gu S.-Q., Joeckel J., Rodnina M.V., Bukau B., Wintermeyer W.
      Proc. Natl. Acad. Sci. U.S.A. 101:7902-7906(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMULTANEOUS BINDING OF TRIGGER FACTOR AND SRP TO THE RIBOSOME.
      Strain: MRE-600.
    15. "Early targeting events during membrane protein biogenesis in Escherichia coli."
      Bibi E.
      Biochim. Biophys. Acta 1808:841-850(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    16. "Structure of a methionine-rich segment of Escherichia coli Ffh protein."
      Oh D.-B., Yi G.-S., Chi S.-W., Kim H.
      FEBS Lett. 395:160-164(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 410-434.
    17. "Crystal structure of the ribonucleoprotein core of the signal recognition particle."
      Batey R.T., Rambo R.P., Lucast L., Rha B., Doudna J.A.
      Science 287:1232-1239(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 371-430 IN COMPLEX WITH 4.5S RNA, DOMAIN.
    18. "Structural and energetic analysis of metal ions essential to SRP signal recognition domain assembly."
      Batey R.T., Doudna J.A.
      Biochemistry 41:11703-11710(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 328-432, SUBUNIT.
    19. "Following the signal sequence from ribosomal tunnel exit to signal recognition particle."
      Halic M., Blau M., Becker T., Mielke T., Pool M.R., Wild K., Sinning I., Beckmann R.
      Nature 444:507-511(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (8.00 ANGSTROMS) OF 2-431.
    20. "A general strategy to solve the phase problem in RNA crystallography."
      Keel A.Y., Rambo R.P., Batey R.T., Kieft J.S.
      Structure 15:761-772(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 329-430.
    21. "Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor."
      Estrozi L.F., Boehringer D., Shan S.O., Ban N., Schaffitzel C.
      Nat. Struct. Mol. Biol. 18:88-90(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (13.50 ANGSTROMS) OF 371-430.
    22. "The crystal structure of the signal recognition particle in complex with its receptor."
      Ataide S.F., Schmitz N., Shen K., Ke A., Shan S.O., Doudna J.A., Ban N.
      Science 331:881-886(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.94 ANGSTROMS) OF 1-433.

    Entry informationi

    Entry nameiSRP54_ECOLI
    AccessioniPrimary (citable) accession number: P0AGD7
    Secondary accession number(s): P07019, P77007, P77008
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 90 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