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Protein

Signal recognition particle receptor FtsY

Gene

ftsY

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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.UniRule annotation6 Publications

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)DescriptionActionsGraphical viewLength
Nucleotide bindingi300 – 307GTPUniRule annotation8
Nucleotide bindingi382 – 386GTPUniRule annotation5
Nucleotide bindingi446 – 449GTPUniRule annotation4

GO - Molecular functioni

  • GTPase activity Source: EcoCyc
  • GTP binding Source: EcoCyc

GO - Biological processi

  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10346. ftsY.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi14G → A: Blocks proteolytic cleavage and impairs activity in cotranslational targeting. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001011312 – 497Signal recognition particle receptor FtsYAdd BLAST496

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei14 – 15Cleavage1 Publication2

Proteomic databases

EPDiP10121.
PaxDbiP10121.
PRIDEiP10121.

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.UniRule annotation2 Publications

Protein-protein interaction databases

BioGridi4262499. 510 interactors.
DIPiDIP-9709N.
IntActiP10121. 6 interactors.
MINTiMINT-1247716.
STRINGi511145.b3464.

Structurei

Secondary structure

1497
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi192 – 202Combined sources11
Helixi204 – 207Combined sources4
Helixi211 – 213Combined sources3
Helixi214 – 218Combined sources5
Helixi225 – 237Combined sources13
Helixi242 – 259Combined sources18
Helixi264 – 266Combined sources3
Helixi267 – 280Combined sources14
Beta strandi294 – 299Combined sources6
Helixi306 – 319Combined sources14
Beta strandi324 – 327Combined sources4
Helixi334 – 347Combined sources14
Helixi360 – 373Combined sources14
Beta strandi377 – 381Combined sources5
Helixi387 – 389Combined sources3
Helixi390 – 405Combined sources16
Beta strandi412 – 420Combined sources9
Helixi421 – 424Combined sources4
Helixi425 – 437Combined sources13
Beta strandi441 – 446Combined sources6
Helixi448 – 450Combined sources3
Turni452 – 455Combined sources4
Helixi456 – 464Combined sources9
Beta strandi468 – 472Combined sources5
Beta strandi474 – 476Combined sources3
Helixi477 – 479Combined sources3
Beta strandi480 – 482Combined sources3
Helixi485 – 493Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5GADelectron microscopy3.70l1-497[»]
ProteinModelPortaliP10121.
SMRiP10121.
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).UniRule annotation7 Publications

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CCP. Bacteria.
COG0552. LUCA.
HOGENOMiHOG000036278.
InParanoidiP10121.
KOiK03110.
OMAiEGQKQET.
PhylomeDBiP10121.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00920. FtsY. 1 hit.
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.
WP_001040654.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76489; AAC76489; b3464.
BAE77829; BAE77829; BAE77829.
GeneIDi947978.
KEGGiecj:JW3429.
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.
PIRiS03130. CEECFY.
RefSeqiNP_417921.1. NC_000913.3.
WP_001040654.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5GADelectron microscopy3.70l1-497[»]
ProteinModelPortaliP10121.
SMRiP10121.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262499. 510 interactors.
DIPiDIP-9709N.
IntActiP10121. 6 interactors.
MINTiMINT-1247716.
STRINGi511145.b3464.

Protein family/group databases

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

Proteomic databases

EPDiP10121.
PaxDbiP10121.
PRIDEiP10121.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76489; AAC76489; b3464.
BAE77829; BAE77829; BAE77829.
GeneIDi947978.
KEGGiecj:JW3429.
eco:b3464.
PATRICi32122372. VBIEscCol129921_3563.

Organism-specific databases

EchoBASEiEB0342.
EcoGeneiEG10346. ftsY.

Phylogenomic databases

eggNOGiENOG4105CCP. Bacteria.
COG0552. LUCA.
HOGENOMiHOG000036278.
InParanoidiP10121.
KOiK03110.
OMAiEGQKQET.
PhylomeDBiP10121.

Enzyme and pathway databases

BioCyciEcoCyc:EG10346-MONOMER.
ECOL316407:JW3429-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP10121.
PROiP10121.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00920. FtsY. 1 hit.
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]
ProtoNetiSearch...

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 2, 2016
This is version 160 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.