P10121 (FTSY_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Signal recognition particle receptor FtsY
Short name=SRP receptor

Gene names

Name:	ftsY
Ordered Locus Names:	b3464, JW3429

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	497 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Cytoplasm Membrane
Ligand	GTP-binding Nucleotide-binding
Molecular function	Receptor
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	SRP-dependent cotranslational protein targeting to membrane Inferred from direct assay PubMed 8107852. Source: EcoCyc
Cellular_component	cytosol Inferred from direct assay Ref.7. Source: EcoCyc intrinsic to plasma membrane Inferred from direct assay Ref.16PubMed 8107852. Source: EcoCyc
Molecular_function	GTP binding Inferred from direct assay PubMed 8107852. Source: EcoCyc GTPase activity Inferred from direct assay PubMed 8107852. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 497

496

Signal recognition particle receptor FtsY HAMAP-Rule MF_00920

PRO_0000101131

Regions

Nucleotide binding

300 – 307

8

GTP By similarity

Nucleotide binding

382 – 386

5

GTP By similarity

Nucleotide binding

446 – 449

4

GTP By similarity

Sites

Site

14 – 15

2

Cleavage

Experimental info

Mutagenesis

14

1

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

Secondary structure

1

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497

Helix Strand Turn

Details...

Helix

192 – 202

11

Helix

204 – 207

4

Helix

211 – 213

3

Helix

214 – 218

5

Helix

225 – 237

13

Helix

242 – 259

18

Helix

264 – 266

3

Helix

267 – 280

14

Beta strand

294 – 299

6

Helix

306 – 319

14

Beta strand

324 – 327

4

Helix

334 – 347

14

Helix

360 – 373

14

Beta strand

377 – 381

5

Helix

387 – 389

3

Helix

390 – 405

16

Beta strand

412 – 420

9

Helix

421 – 424

4

Helix

425 – 437

13

Beta strand

441 – 446

6

Helix

448 – 450

3

Turn

452 – 455

4

Helix

456 – 464

9

Beta strand

468 – 472

5

Beta strand

474 – 476

3

Helix

477 – 479

3

Beta strand

480 – 482

3

Helix

485 – 493

9

Sequences

	Sequence		Length	Mass (Da)
	P10121 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: EBE640072B5D1021	FASTA	497	54,513
	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

References

	« Hide 'large scale' referencesShow '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 277:1453-1474(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.

PIR

CEECFY. S03130.

RefSeq

NP_417921.1. NC_000913.2.
YP_491970.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P10121.

SMR

P10121. Positions 188-495.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9709N.

IntAct

P10121. 5 interactions.

MINT

MINT-1247716.

STRING

511145.b3464.

Protein family/group databases

TCDB

3.A.5.1.1. general secretory pathway (Sec) family.

Proteomic databases

PaxDb

P10121.

PRIDE

P10121.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76489; AAC76489; b3464.
BAE77829; BAE77829; BAE77829.

GeneID

12933505.
947978.

KEGG

ecj:Y75_p3714.
eco:b3464.

PATRIC

32122372. VBIEscCol129921_3563.

Organism-specific databases

EchoBASE

EB0342.

EcoGene

EG10346. ftsY.

Phylogenomic databases

eggNOG

COG0552.

HOGENOM

HOG000036278.

KO

K03110.

OMA

AETNAEY.

ProtClustDB

PRK10416.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P10121.

Family and domain databases

HAMAP

MF_00920. FtsY.

InterPro

IPR003593. AAA+_ATPase.
IPR013822. Signal_recog_particl_SRP54_hlx.
IPR004390. SR_rcpt_FtsY.
IPR000897. SRP54_GTPase_dom.
[Graphical view]

Pfam

PF00448. SRP54. 1 hit.
PF02881. SRP54_N. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
SM00962. SRP54. 1 hit.
SM00963. SRP54_N. 1 hit.
[Graphical view]

SUPFAM

SSF47364. SRP54. 1 hit.

TIGRFAMs

TIGR00064. ftsY. 1 hit.

PROSITE

PS00300. SRP54. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P10121.

Entry information

Entry name

FTSY_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 132 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program