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P10121

- FTSY_ECOLI

UniProt

P10121 - FTSY_ECOLI

Protein

Signal recognition particle receptor FtsY

Gene

ftsY

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 143 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC 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.6 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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei14 – 152Cleavage

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi300 – 3078GTPUniRule annotation
    Nucleotide bindingi382 – 3865GTPUniRule annotation
    Nucleotide bindingi446 – 4494GTPUniRule annotation

    GO - Molecular functioni

    1. GTPase activity Source: EcoCyc
    2. GTP binding Source: EcoCyc

    GO - Biological processi

    1. SRP-dependent cotranslational protein targeting to membrane Source: EcoCyc

    Keywords - Molecular functioni

    Receptor

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10346-MONOMER.
    ECOL316407:JW3429-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 receptor FtsYUniRule annotation
    Short name:
    SRP receptorUniRule annotation
    Gene namesi
    Name:ftsYUniRule annotation
    Ordered Locus Names:b3464, JW3429
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10346. ftsY.

    Subcellular locationi

    Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm
    Note: Distributed between the membrane and the cytoplasm. Binding to the membrane probably occurs initially through phospholipid binding, which allows a strong membrane contact, followed by interaction with a membrane protein. Targeting of FtsY to the membrane is essential for proper function. The stability of this membrane contact may be regulated by cleavage of helix 1.

    GO - Cellular componenti

    1. cytosol Source: EcoCyc
    2. intrinsic component of plasma membrane Source: EcoCyc

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Deletion affects both cell morphology and protein export. Mutants are defective in the insertion into the cytoplasmic membrane of three topologically distinct membrane proteins, MalF, AcrB and FtsQ.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141G → A: Blocks proteolytic cleavage and impairs activity in cotranslational targeting. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 497496Signal recognition particle receptor FtsYPRO_0000101131Add
    BLAST

    Post-translational modificationi

    Proteolytically cleaved. The cleavage may regulate function and subcellular location of FtsY. Full-length FtsY is found primarily associated with the membrane, while cleaved protein is predominantly present in the cytoplasm.1 Publication

    Proteomic databases

    PaxDbiP10121.
    PRIDEiP10121.

    Expressioni

    Gene expression databases

    GenevestigatoriP10121.

    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. Binds to SecY.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    DIPiDIP-9709N.
    IntActiP10121. 6 interactions.
    MINTiMINT-1247716.
    STRINGi511145.b3464.

    Structurei

    Secondary structure

    1
    497
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi192 – 20211
    Helixi204 – 2074
    Helixi211 – 2133
    Helixi214 – 2185
    Helixi225 – 23713
    Helixi242 – 25918
    Helixi264 – 2663
    Helixi267 – 28014
    Beta strandi294 – 2996
    Helixi306 – 31914
    Beta strandi324 – 3274
    Helixi334 – 34714
    Helixi360 – 37314
    Beta strandi377 – 3815
    Helixi387 – 3893
    Helixi390 – 40516
    Beta strandi412 – 4209
    Helixi421 – 4244
    Helixi425 – 43713
    Beta strandi441 – 4466
    Helixi448 – 4503
    Turni452 – 4554
    Helixi456 – 4649
    Beta strandi468 – 4725
    Beta strandi474 – 4763
    Helixi477 – 4793
    Beta strandi480 – 4823
    Helixi485 – 4939

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FTSX-ray2.20A201-495[»]
    2QY9X-ray1.90A196-497[»]
    2XXAX-ray3.94B/D196-497[»]
    2YHSX-ray1.60A1-497[»]
    3ZN8electron microscopy12.00D201-495[»]
    4C7OX-ray2.60B/D224-497[»]
    ProteinModelPortaliP10121.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10121.

    Family & Domainsi

    Domaini

    Contains an acidic N-terminal A domain, a central N domain and a C-terminal GTPase G domain that can bind and hydrolyze GTP. Contains at least two lipid-binding sites. The first site contains the first 14 amino acids (helix 1) and the second binding site is an amphipathic alpha-helix located at the interface between the A- and the N-domain (helix 2).7 PublicationsUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0552.
    HOGENOMiHOG000036278.
    KOiK03110.
    OMAiPKTHTEA.
    OrthoDBiEOG62K1ZH.
    PhylomeDBiP10121.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00920. FtsY.
    InterProiIPR003593. AAA+_ATPase.
    IPR027417. P-loop_NTPase.
    IPR013822. Signal_recog_particl_SRP54_hlx.
    IPR004390. SR_rcpt_FtsY.
    IPR000897. SRP54_GTPase_dom.
    [Graphical view]
    PfamiPF00448. SRP54. 1 hit.
    PF02881. SRP54_N. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM00962. SRP54. 1 hit.
    SM00963. SRP54_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47364. SSF47364. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00064. ftsY. 1 hit.
    PROSITEiPS00300. SRP54. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P10121-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKEKKRGFF SWLGFGQKEQ TPEKETEVQN EQPVVEEIVQ AQEPVKASEQ    50
    AVEEQPQAHT EAEAETFAAD VVEVTEQVAE SEKAQPEAEV VAQPEPVVEE 100
    TPEPVAIERE ELPLPEDVNA EAVSPEEWQA EAETVEIVEA AEEEAAKEEI 150
    TDEELETALA AEAAEEAVMV VPPAEEEQPV EEIAQEQEKP TKEGFFARLK 200
    RSLLKTKENL GSGFISLFRG KKIDDDLFEE LEEQLLIADV GVETTRKIIT 250
    NLTEGASRKQ LRDAEALYGL LKEEMGEILA KVDEPLNVEG KAPFVILMVG 300
    VNGVGKTTTI GKLARQFEQQ GKSVMLAAGD TFRAAAVEQL QVWGQRNNIP 350
    VIAQHTGADS ASVIFDAIQA AKARNIDVLI ADTAGRLQNK SHLMEELKKI 400
    VRVMKKLDVE APHEVMLTID ASTGQNAVSQ AKLFHEAVGL TGITLTKLDG 450
    TAKGGVIFSV ADQFGIPIRY IGVGERIEDL RPFKADDFIE ALFARED 497
    Length:497
    Mass (Da):54,513
    Last modified:July 1, 1989 - v1
    Checksum:iEBE640072B5D1021
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04398 Genomic DNA. Translation: CAA27984.1.
    U00039 Genomic DNA. Translation: AAB18439.1.
    U00096 Genomic DNA. Translation: AAC76489.1.
    AP009048 Genomic DNA. Translation: BAE77829.1.
    PIRiS03130. CEECFY.
    RefSeqiNP_417921.1. NC_000913.3.
    YP_491970.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76489; AAC76489; b3464.
    BAE77829; BAE77829; BAE77829.
    GeneIDi12933505.
    947978.
    KEGGiecj:Y75_p3714.
    eco:b3464.
    PATRICi32122372. VBIEscCol129921_3563.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04398 Genomic DNA. Translation: CAA27984.1 .
    U00039 Genomic DNA. Translation: AAB18439.1 .
    U00096 Genomic DNA. Translation: AAC76489.1 .
    AP009048 Genomic DNA. Translation: BAE77829.1 .
    PIRi S03130. CEECFY.
    RefSeqi NP_417921.1. NC_000913.3.
    YP_491970.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FTS X-ray 2.20 A 201-495 [» ]
    2QY9 X-ray 1.90 A 196-497 [» ]
    2XXA X-ray 3.94 B/D 196-497 [» ]
    2YHS X-ray 1.60 A 1-497 [» ]
    3ZN8 electron microscopy 12.00 D 201-495 [» ]
    4C7O X-ray 2.60 B/D 224-497 [» ]
    ProteinModelPortali P10121.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9709N.
    IntActi P10121. 6 interactions.
    MINTi MINT-1247716.
    STRINGi 511145.b3464.

    Protein family/group databases

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

    Proteomic databases

    PaxDbi P10121.
    PRIDEi P10121.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76489 ; AAC76489 ; b3464 .
    BAE77829 ; BAE77829 ; BAE77829 .
    GeneIDi 12933505.
    947978.
    KEGGi ecj:Y75_p3714.
    eco:b3464.
    PATRICi 32122372. VBIEscCol129921_3563.

    Organism-specific databases

    EchoBASEi EB0342.
    EcoGenei EG10346. ftsY.

    Phylogenomic databases

    eggNOGi COG0552.
    HOGENOMi HOG000036278.
    KOi K03110.
    OMAi PKTHTEA.
    OrthoDBi EOG62K1ZH.
    PhylomeDBi P10121.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10346-MONOMER.
    ECOL316407:JW3429-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P10121.
    PROi P10121.

    Gene expression databases

    Genevestigatori P10121.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    HAMAPi MF_00920. FtsY.
    InterProi IPR003593. AAA+_ATPase.
    IPR027417. P-loop_NTPase.
    IPR013822. Signal_recog_particl_SRP54_hlx.
    IPR004390. SR_rcpt_FtsY.
    IPR000897. SRP54_GTPase_dom.
    [Graphical view ]
    Pfami PF00448. SRP54. 1 hit.
    PF02881. SRP54_N. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    SM00962. SRP54. 1 hit.
    SM00963. SRP54_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47364. SSF47364. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00064. ftsY. 1 hit.
    PROSITEi PS00300. SRP54. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A new cell division operon in Escherichia coli."
      Gill D.R., Hatfull G.F., Salmond G.P.C.
      Mol. Gen. Genet. 205:134-145(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
      Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
      Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    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].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "A cleavable N-terminal membrane anchor is involved in membrane binding of the Escherichia coli SRP receptor."
      Weiche B., Burk J., Angelini S., Schiltz E., Thumfart J.O., Koch H.G.
      J. Mol. Biol. 377:761-773(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11 AND 15-25, SUBCELLULAR LOCATION, DOMAIN, CLEAVAGE, MUTAGENESIS OF GLY-14.
    6. "The identification of the Escherichia coli ftsY gene product: an unusual protein."
      Gill D.R., Salmond G.P.C.
      Mol. Microbiol. 4:575-583(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. "An alternative protein targeting pathway in Escherichia coli: studies on the role of FtsY."
      Luirink J., ten Hagen-Jongman C.M., van der Weijden C.C., Oudega B., High S., Dobberstein B., Kusters R.
      EMBO J. 13:2289-2296(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    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, DOMAIN.
    9. "The NG domain of the prokaryotic signal recognition particle receptor, FtsY, is fully functional when fused to an unrelated integral membrane polypeptide."
      Zelazny A., Seluanov A., Cooper A., Bibi E.
      Proc. Natl. Acad. Sci. U.S.A. 94:6025-6029(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DOMAIN.
    10. "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.
    11. "FtsY binds to the Escherichia coli inner membrane via interactions with phosphatidylethanolamine and membrane proteins."
      Millman J.S., Qi H.Y., Vulcu F., Bernstein H.D., Andrews D.W.
      J. Biol. Chem. 276:25982-25989(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "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.
    13. "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: FUNCTION, BINDING OF FTSY AND SRP TO THE RIBOSOME.
      Strain: MRE-600.
    14. "Membrane targeting of ribosomes and their release require distinct and separable functions of FtsY."
      Bahari L., Parlitz R., Eitan A., Stjepanovic G., Bochkareva E.S., Sinning I., Bibi E.
      J. Biol. Chem. 282:32168-32175(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DOMAIN.
    15. "Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation."
      Shan S.O., Chandrasekar S., Walter P.
      J. Cell Biol. 178:611-620(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, GTPASE ACTIVITY.
    16. "Two cooperating helices constitute the lipid-binding domain of the bacterial SRP receptor."
      Braig D., Bar C., Thumfart J.O., Koch H.G.
      J. Mol. Biol. 390:401-413(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, LIPID-BINDING SITES, SUBCELLULAR LOCATION.
    17. "The bacterial SRP receptor, SecA and the ribosome use overlapping binding sites on the SecY translocon."
      Kuhn P., Weiche B., Sturm L., Sommer E., Drepper F., Warscheid B., Sourjik V., Koch H.G.
      Traffic 12:563-578(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SECY.
    18. "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.
    19. "Crystal structure of the NG domain from the signal-recognition particle receptor FtsY."
      Montoya G., Svensson C., Luirink J., Sinning I.
      Nature 385:365-368(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 201-495, DOMAIN.
    20. "Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix."
      Parlitz R., Eitan A., Stjepanovic G., Bahari L., Bange G., Bibi E., Sinning I.
      J. Biol. Chem. 282:32176-32184(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 196-497, DOMAIN.
    21. "Lipids trigger a conformational switch that regulates signal recognition particle (SRP)-mediated protein targeting."
      Stjepanovic G., Kapp K., Bange G., Graf C., Parlitz R., Wild K., Mayer M.P., Sinning I.
      J. Biol. Chem. 286:23489-23497(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), SUBCELLULAR LOCATION.
    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 196-497 IN COMPLEX WITH SRP.

    Entry informationi

    Entry nameiFTSY_ECOLI
    AccessioniPrimary (citable) accession number: P10121
    Secondary accession number(s): Q2M7C7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 143 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3