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P10121

- FTSY_ECOLI

UniProt

P10121 - FTSY_ECOLI

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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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 20211Combined sources
Helixi204 – 2074Combined sources
Helixi211 – 2133Combined sources
Helixi214 – 2185Combined sources
Helixi225 – 23713Combined sources
Helixi242 – 25918Combined sources
Helixi264 – 2663Combined sources
Helixi267 – 28014Combined sources
Beta strandi294 – 2996Combined sources
Helixi306 – 31914Combined sources
Beta strandi324 – 3274Combined sources
Helixi334 – 34714Combined sources
Helixi360 – 37314Combined sources
Beta strandi377 – 3815Combined sources
Helixi387 – 3893Combined sources
Helixi390 – 40516Combined sources
Beta strandi412 – 4209Combined sources
Helixi421 – 4244Combined sources
Helixi425 – 43713Combined sources
Beta strandi441 – 4466Combined sources
Helixi448 – 4503Combined sources
Turni452 – 4554Combined sources
Helixi456 – 4649Combined sources
Beta strandi468 – 4725Combined sources
Beta strandi474 – 4763Combined sources
Helixi477 – 4793Combined sources
Beta strandi480 – 4823Combined sources
Helixi485 – 4939Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
SMRiP10121. Positions 188-495.
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.
InParanoidiP10121.
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

        10         20         30         40         50
MAKEKKRGFF SWLGFGQKEQ TPEKETEVQN EQPVVEEIVQ AQEPVKASEQ
60 70 80 90 100
AVEEQPQAHT EAEAETFAAD VVEVTEQVAE SEKAQPEAEV VAQPEPVVEE
110 120 130 140 150
TPEPVAIERE ELPLPEDVNA EAVSPEEWQA EAETVEIVEA AEEEAAKEEI
160 170 180 190 200
TDEELETALA AEAAEEAVMV VPPAEEEQPV EEIAQEQEKP TKEGFFARLK
210 220 230 240 250
RSLLKTKENL GSGFISLFRG KKIDDDLFEE LEEQLLIADV GVETTRKIIT
260 270 280 290 300
NLTEGASRKQ LRDAEALYGL LKEEMGEILA KVDEPLNVEG KAPFVILMVG
310 320 330 340 350
VNGVGKTTTI GKLARQFEQQ GKSVMLAAGD TFRAAAVEQL QVWGQRNNIP
360 370 380 390 400
VIAQHTGADS ASVIFDAIQA AKARNIDVLI ADTAGRLQNK SHLMEELKKI
410 420 430 440 450
VRVMKKLDVE APHEVMLTID ASTGQNAVSQ AKLFHEAVGL TGITLTKLDG
460 470 480 490
TAKGGVIFSV ADQFGIPIRY IGVGERIEDL RPFKADDFIE ALFARED
Length:497
Mass (Da):54,513
Last modified:July 1, 1989 - v1
Checksum:iEBE640072B5D1021
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
SMRi P10121. Positions 188-495.
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.
InParanoidi P10121.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 145 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