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Protein

Signal recognition particle protein

Gene

ffh

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY 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 annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi107 – 1148GTPUniRule annotation
Nucleotide bindingi190 – 1945GTPUniRule annotation
Nucleotide bindingi248 – 2514GTPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

GTP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciECOL386585:GJFA-3439-MONOMER.
ECOO157:FFH-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal recognition particle proteinUniRule annotation
Alternative name(s):
Fifty-four homologUniRule annotation
Gene namesi
Name:ffhUniRule annotation
Ordered Locus Names:Z3904, ECs3473
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

  • Note: The SRP-RNC complex is targeted to the cytoplasmic membrane.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Signal recognition particle

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453Signal recognition particle proteinPRO_0000101154Add
BLAST

Proteomic databases

PRIDEiP0AGD9.

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.UniRule annotation

Protein-protein interaction databases

MINTiMINT-1218587.
STRINGi155864.Z3904.

Structurei

3D structure databases

ProteinModelPortaliP0AGD9.
SMRiP0AGD9. Positions 2-431.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC.UniRule annotation

Sequence similaritiesi

Belongs to the GTP-binding SRP family. SRP54 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CB9. Bacteria.
COG0541. LUCA.
HOGENOMiHOG000036164.
KOiK03106.
OMAiMLPGMGQ.

Family and domain databases

Gene3Di1.10.260.30. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00306. SRP54. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR013822. Signal_recog_particl_SRP54_hlx.
IPR004125. Signal_recog_particle_SRP54_M.
IPR022941. SRP54.
IPR000897. SRP54_GTPase_dom.
IPR004780. SRP_Ffh.
[Graphical view]
PANTHERiPTHR11564:SF7. PTHR11564:SF7. 1 hit.
PfamiPF00448. SRP54. 1 hit.
PF02881. SRP54_N. 1 hit.
PF02978. SRP_SPB. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00962. SRP54. 1 hit.
SM00963. SRP54_N. 1 hit.
[Graphical view]
SUPFAMiSSF47446. SSF47446. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00959. ffh. 1 hit.
PROSITEiPS00300. SRP54. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AGD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFDNLTDRLS RTLRNISGRG RLTEDNVKDT LREVRMALLE ADVALPVVRE
60 70 80 90 100
FINRVKEKAV GHEVNKSLTP GQEFVKIVRN ELVAAMGEEN QTLNLAAQPP
110 120 130 140 150
AVVLMAGLQG AGKTTSVGKL GKFLREKHKK KVLVVSADVY RPAAIKQLET
160 170 180 190 200
LAEQVGVDFF PSDVGQKPVD IVNAALKEAK LKFYDVLLVD TAGRLHVDEA
210 220 230 240 250
MMDEIKQVHA SINPVETLFV VDAMTGQDAA NTAKAFNEAL PLTGVVLTKV
260 270 280 290 300
DGDARGGAAL SIRHITGKPI KFLGVGEKTE ALEPFHPDRI ASRILGMGDV
310 320 330 340 350
LSLIEDIESK VDRAQAEKLA SKLKKGDGFD LNDFLEQLRQ MKNMGGMASL
360 370 380 390 400
MGKLPGMGQI PDNVKSQMDD KVLVRMEAII NSMTMKERAK PEIIKGSRKR
410 420 430 440 450
RIAAGCGMQV QDVNRLLKQF DDMQRMMKKM KKGGMAKMMR SMKGMMPPGF

PGR
Length:453
Mass (Da):49,787
Last modified:December 20, 2005 - v1
Checksum:iE9C7A7101CC04D66
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57721.1.
BA000007 Genomic DNA. Translation: BAB36896.1.
PIRiA91063.
E85907.
RefSeqiNP_311500.1. NC_002695.1.
WP_000460035.1. NZ_LPWC01000002.1.

Genome annotation databases

EnsemblBacteriaiAAG57721; AAG57721; Z3904.
BAB36896; BAB36896; BAB36896.
GeneIDi914815.
KEGGiece:Z3904.
ecs:ECs3473.
PATRICi18356390. VBIEscCol44059_3385.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG57721.1.
BA000007 Genomic DNA. Translation: BAB36896.1.
PIRiA91063.
E85907.
RefSeqiNP_311500.1. NC_002695.1.
WP_000460035.1. NZ_LPWC01000002.1.

3D structure databases

ProteinModelPortaliP0AGD9.
SMRiP0AGD9. Positions 2-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1218587.
STRINGi155864.Z3904.

Proteomic databases

PRIDEiP0AGD9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG57721; AAG57721; Z3904.
BAB36896; BAB36896; BAB36896.
GeneIDi914815.
KEGGiece:Z3904.
ecs:ECs3473.
PATRICi18356390. VBIEscCol44059_3385.

Phylogenomic databases

eggNOGiENOG4105CB9. Bacteria.
COG0541. LUCA.
HOGENOMiHOG000036164.
KOiK03106.
OMAiMLPGMGQ.

Enzyme and pathway databases

BioCyciECOL386585:GJFA-3439-MONOMER.
ECOO157:FFH-MONOMER.

Family and domain databases

Gene3Di1.10.260.30. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00306. SRP54. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR013822. Signal_recog_particl_SRP54_hlx.
IPR004125. Signal_recog_particle_SRP54_M.
IPR022941. SRP54.
IPR000897. SRP54_GTPase_dom.
IPR004780. SRP_Ffh.
[Graphical view]
PANTHERiPTHR11564:SF7. PTHR11564:SF7. 1 hit.
PfamiPF00448. SRP54. 1 hit.
PF02881. SRP54_N. 1 hit.
PF02978. SRP_SPB. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00962. SRP54. 1 hit.
SM00963. SRP54_N. 1 hit.
[Graphical view]
SUPFAMiSSF47446. SSF47446. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00959. ffh. 1 hit.
PROSITEiPS00300. SRP54. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSRP54_ECO57
AccessioniPrimary (citable) accession number: P0AGD9
Secondary accession number(s): P07019, P77007, P77008
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: December 20, 2005
Last modified: September 7, 2016
This is version 79 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

Complete proteome

Documents

  1. 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.