Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P10121 (FTSY_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal recognition particle receptor FtsY

Short name=SRP receptor
Gene names
Name:ftsY
Ordered Locus Names:b3464, JW3429
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.8 Ref.10 Ref.12 Ref.13 Ref.15

Enzyme regulation

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. Ref.10

Subunit structure

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. Ref.8

Subcellular location

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. Ref.5 Ref.7 Ref.9 Ref.11 Ref.14 Ref.16 Ref.21

Domain

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). Ref.5 Ref.8 Ref.9 Ref.14 Ref.16 Ref.19 Ref.20

Post-translational modification

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. Ref.5

Disruption phenotype

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. Ref.7 Ref.12

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 497496Signal recognition particle receptor FtsY HAMAP-Rule MF_00920
PRO_0000101131

Regions

Nucleotide binding300 – 3078GTP By similarity
Nucleotide binding382 – 3865GTP By similarity
Nucleotide binding446 – 4494GTP By similarity

Sites

Site14 – 152Cleavage

Experimental info

Mutagenesis141G → A: Blocks proteolytic cleavage and impairs activity in cotranslational targeting. Ref.5

Secondary structure

................................................. 497
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10121 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: EBE640072B5D1021

FASTA49754,513
        10         20         30         40         50         60 
MAKEKKRGFF SWLGFGQKEQ TPEKETEVQN EQPVVEEIVQ AQEPVKASEQ AVEEQPQAHT 

        70         80         90        100        110        120 
EAEAETFAAD VVEVTEQVAE SEKAQPEAEV VAQPEPVVEE TPEPVAIERE ELPLPEDVNA 

       130        140        150        160        170        180 
EAVSPEEWQA EAETVEIVEA AEEEAAKEEI TDEELETALA AEAAEEAVMV VPPAEEEQPV 

       190        200        210        220        230        240 
EEIAQEQEKP TKEGFFARLK RSLLKTKENL GSGFISLFRG KKIDDDLFEE LEEQLLIADV 

       250        260        270        280        290        300 
GVETTRKIIT NLTEGASRKQ LRDAEALYGL LKEEMGEILA KVDEPLNVEG KAPFVILMVG 

       310        320        330        340        350        360 
VNGVGKTTTI GKLARQFEQQ GKSVMLAAGD TFRAAAVEQL QVWGQRNNIP VIAQHTGADS 

       370        380        390        400        410        420 
ASVIFDAIQA AKARNIDVLI ADTAGRLQNK SHLMEELKKI VRVMKKLDVE APHEVMLTID 

       430        440        450        460        470        480 
ASTGQNAVSQ AKLFHEAVGL TGITLTKLDG TAKGGVIFSV ADQFGIPIRY IGVGERIEDL 

       490 
RPFKADDFIE ALFARED 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04398 Genomic DNA. Translation: CAA27984.1.
U00039 Genomic DNA. Translation: AAB18439.1.
U00096 Genomic DNA. Translation: AAC76489.1.
AP009048 Genomic DNA. Translation: BAE77829.1.
PIRCEECFY. S03130.
RefSeqNP_417921.1. NC_000913.3.
YP_491970.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP10121.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9709N.
IntActP10121. 6 interactions.
MINTMINT-1247716.
STRING511145.b3464.

Protein family/group databases

TCDB3.A.5.1.1. the general secretory pathway (sec) family.

Proteomic databases

PaxDbP10121.
PRIDEP10121.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76489; AAC76489; b3464.
BAE77829; BAE77829; BAE77829.
GeneID12933505.
947978.
KEGGecj:Y75_p3714.
eco:b3464.
PATRIC32122372. VBIEscCol129921_3563.

Organism-specific databases

EchoBASEEB0342.
EcoGeneEG10346. ftsY.

Phylogenomic databases

eggNOGCOG0552.
HOGENOMHOG000036278.
KOK03110.
OMAPKTHTEA.
OrthoDBEOG62K1ZH.
PhylomeDBP10121.

Enzyme and pathway databases

BioCycEcoCyc:EG10346-MONOMER.
ECOL316407:JW3429-MONOMER.

Gene expression databases

GenevestigatorP10121.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00920. FtsY.
InterProIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR013822. Signal_recog_particl_SRP54_hlx.
IPR004390. SR_rcpt_FtsY.
IPR000897. SRP54_GTPase_dom.
[Graphical view]
PfamPF00448. SRP54. 1 hit.
PF02881. SRP54_N. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM00962. SRP54. 1 hit.
SM00963. SRP54_N. 1 hit.
[Graphical view]
SUPFAMSSF47364. SSF47364. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00064. ftsY. 1 hit.
PROSITEPS00300. SRP54. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10121.
PROP10121.

Entry information

Entry nameFTSY_ECOLI
AccessionPrimary (citable) accession number: P10121
Secondary accession number(s): Q2M7C7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 11, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene