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Protein

Signal recognition particle receptor FtsY

Gene

ftsY

Organism
Thermus aquaticus
Status
Reviewed-Annotation score: Annotation score: 4 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).UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi109 – 1168GTPUniRule annotation
Nucleotide bindingi191 – 1955GTPUniRule annotation
Nucleotide bindingi255 – 2584GTPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Signal recognition particle receptor FtsYUniRule annotation
Short name:
SRP receptorUniRule annotation
Gene namesi
Name:ftsYUniRule annotation
OrganismiThermus aquaticusImported
Taxonomic identifieri271 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171R → Q: No effect on proteolysis; when associated with M-18. 1 Publication
Mutagenesisi18 – 181L → M: No effect on proteolysis; when associated with Q-17. 1 Publication
Mutagenesisi86 – 861R → Q: No effect proteolysis; when associated with Q-87 and I-88. 1 Publication
Mutagenesisi87 – 871K → Q: No effect proteolysis; when associated with Q-86 and I-88. 1 Publication
Mutagenesisi88 – 881L → I: No effect proteolysis; when associated with Q-86 and Q-87. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 304303Signal recognition particle receptor FtsYPRO_0000101147Add
BLAST

Post-translational modificationi

Sensitive to endogenous proteolytic cleavage between residues 18 and 19 and between residues 86 and 87.

Interactioni

Subunit structurei

Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
ffhO073472EBI-1037899,EBI-1037906

Protein-protein interaction databases

IntActiP83749. 1 interaction.
STRINGi498848.TaqDRAFT_3813.

Structurei

Secondary structure

1
304
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 108Combined sources
Helixi12 – 154Combined sources
Turni16 – 183Combined sources
Helixi19 – 213Combined sources
Helixi28 – 4114Combined sources
Helixi46 – 5813Combined sources
Helixi66 – 727Combined sources
Turni73 – 764Combined sources
Helixi81 – 877Combined sources
Beta strandi101 – 1088Combined sources
Helixi115 – 12713Combined sources
Turni128 – 1303Combined sources
Beta strandi133 – 1364Combined sources
Turni143 – 1464Combined sources
Helixi147 – 15610Combined sources
Beta strandi164 – 1663Combined sources
Helixi169 – 18315Combined sources
Beta strandi186 – 1905Combined sources
Helixi200 – 21617Combined sources
Beta strandi222 – 2298Combined sources
Helixi230 – 2345Combined sources
Helixi235 – 24713Combined sources
Beta strandi250 – 2556Combined sources
Beta strandi259 – 2613Combined sources
Helixi263 – 2653Combined sources
Helixi266 – 2738Combined sources
Beta strandi277 – 2815Combined sources
Beta strandi283 – 2853Combined sources
Helixi286 – 2883Combined sources
Beta strandi289 – 2913Combined sources
Helixi294 – 3018Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OKKX-ray2.05D2-304[»]
1RJ9X-ray1.90A1-304[»]
2CNWX-ray2.39D/E/F21-304[»]
2IYLX-ray2.10D21-304[»]
2J7PX-ray1.97D/E22-304[»]
2Q9AX-ray2.24A/B1-304[»]
2Q9BX-ray2.30A/B1-304[»]
2Q9CX-ray2.20A/B1-304[»]
2XKVelectron microscopy13.50D2-304[»]
ProteinModelPortaliP83749.
SMRiP83749. Positions 1-304.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83749.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CCP. Bacteria.
COG0552. LUCA.

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.

P83749-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFFDRLKAG LAKTRERLLK AIPWGGNLEE VLEELEMALL AADVGLSATE
60 70 80 90 100
EILQEVRASG RKDLKEAVKE KLVGMLEPDE RRATLRKLGF NPQKPKPVEP
110 120 130 140 150
KGRVVLVVGV NGVGKTTTIA KLGRYYQNLG KKVMFCAGDT FRAAGGTQLS
160 170 180 190 200
EWGKRLSIPV IQGPEGTDPA ALAYDAVQAM KARGYDLLFV DTAGRLHTKH
210 220 230 240 250
NLMEELKKVK RAIAKADPEE PKEVWLVLDA VTGQNGLEQA KKFHEAVGLT
260 270 280 290 300
GVIVTKLDGT AKGGVLIPIV RTLKVPIKFV GVGEGPDDLQ PFDPEAFVEA

LLED
Length:304
Mass (Da):33,055
Last modified:January 23, 2007 - v2
Checksum:i51881F90B4780536
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY484668 Genomic DNA. Translation: AAR28967.1.
RefSeqiWP_053767748.1. NZ_LHCI01000106.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY484668 Genomic DNA. Translation: AAR28967.1.
RefSeqiWP_053767748.1. NZ_LHCI01000106.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OKKX-ray2.05D2-304[»]
1RJ9X-ray1.90A1-304[»]
2CNWX-ray2.39D/E/F21-304[»]
2IYLX-ray2.10D21-304[»]
2J7PX-ray1.97D/E22-304[»]
2Q9AX-ray2.24A/B1-304[»]
2Q9BX-ray2.30A/B1-304[»]
2Q9CX-ray2.20A/B1-304[»]
2XKVelectron microscopy13.50D2-304[»]
ProteinModelPortaliP83749.
SMRiP83749. Positions 1-304.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP83749. 1 interaction.
STRINGi498848.TaqDRAFT_3813.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CCP. Bacteria.
COG0552. LUCA.

Miscellaneous databases

EvolutionaryTraceiP83749.

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]
ProtoNetiSearch...

Publicationsi

  1. "Conformational change of the N-domain on formation of the complex between the GTPase domains of Thermus aquaticus Ffh and FtsY."
    Shepotinovskaya I.V., Freymann D.M.
    Biochim. Biophys. Acta 1597:107-114(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6; 19-25 AND 87-93, MUTAGENESIS OF ARG-17; LEU-18; ARG-86; LYS-87 AND LEU-88.
  2. "Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY."
    Shepotinovskaya I.V., Focia P.J., Freymann D.M.
    Acta Crystallogr. D 59:1834-1837(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiFTSY_THEAQ
AccessioniPrimary (citable) accession number: P83749
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.