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Protein

Signal recognition particle protein

Gene

ffh

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. 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 annotation7 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 bindingi107 – 114GTPUniRule annotation8
Nucleotide bindingi190 – 194GTPUniRule annotation5
Nucleotide bindingi248 – 251GTPUniRule annotation4

GO - Molecular functioni

  • 7S RNA binding Source: InterPro
  • GTPase activity Source: EcoCyc
  • GTP binding Source: EcoliWiki

GO - Biological processi

  • protein targeting to membrane Source: EcoliWiki
  • SRP-dependent cotranslational protein targeting to membrane Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

GTP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10300-MONOMER.
ECOL316407:JW5414-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 proteinUniRule annotation
Alternative name(s):
Fifty-four homologUniRule annotation
Short name:
Ffh
p48
Gene namesi
Name:ffhUniRule annotation
Ordered Locus Names:b2610, JW5414
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10300. ffh.

Subcellular locationi

  • Cytoplasm

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

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • intracellular ribonucleoprotein complex Source: EcoliWiki
  • signal recognition particle Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Signal recognition particle

Pathology & Biotechi

Disruption phenotypei

Essential; deletion experiments lead to loss of inner membrane protein targeting. Also leads to reduced targeting of lipoproteins Lpp and BRP.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001011531 – 453Signal recognition particle proteinAdd BLAST453

Proteomic databases

EPDiP0AGD7.
PaxDbiP0AGD7.
PRIDEiP0AGD7.

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. Metal ions are essential for the formation and stability of the SRP complex. Interacts with the ribosomes, via ribosomal protein L23. Interacts with FtsY.UniRule annotation7 Publications

Protein-protein interaction databases

BioGridi4262086. 262 interactors.
DIPiDIP-31865N.
IntActiP0AGD7. 19 interactors.
MINTiMINT-1218614.
STRINGi511145.b2610.

Structurei

Secondary structure

1453
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 15Combined sources11
Helixi24 – 40Combined sources17
Helixi45 – 60Combined sources16
Helixi70 – 86Combined sources17
Beta strandi96 – 106Combined sources11
Helixi113 – 126Combined sources14
Beta strandi132 – 136Combined sources5
Helixi144 – 155Combined sources12
Beta strandi158 – 160Combined sources3
Helixi168 – 181Combined sources14
Beta strandi185 – 190Combined sources6
Helixi199 – 212Combined sources14
Beta strandi215 – 222Combined sources8
Helixi229 – 239Combined sources11
Beta strandi244 – 248Combined sources5
Helixi258 – 266Combined sources9
Beta strandi270 – 274Combined sources5
Beta strandi276 – 278Combined sources3
Beta strandi282 – 284Combined sources3
Helixi287 – 295Combined sources9
Helixi331 – 338Combined sources8
Helixi373 – 381Combined sources9
Helixi385 – 389Combined sources5
Helixi391 – 393Combined sources3
Helixi396 – 405Combined sources10
Helixi410 – 430Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DULX-ray1.80A329-430[»]
1HQ1X-ray1.52A328-432[»]
2J28electron microscopy8.0092-431[»]
2PXBX-ray2.00A329-430[»]
2PXDX-ray2.00A329-430[»]
2PXEX-ray2.00A329-430[»]
2PXFX-ray2.00A329-430[»]
2PXKX-ray2.00A329-430[»]
2PXLX-ray2.50A329-430[»]
2PXPX-ray2.50A329-430[»]
2PXQX-ray2.50A329-430[»]
2PXTX-ray2.50A329-430[»]
2PXUX-ray2.50A329-430[»]
2PXVX-ray2.00A329-430[»]
2XKVelectron microscopy13.50C329-430[»]
2XXAX-ray3.94A/C1-433[»]
3LQXX-ray1.93A329-428[»]
4C7OX-ray2.60A/C1-298[»]
5AKAelectron microscopy5.705328-436[»]
5GADelectron microscopy3.70i4-434[»]
5GAFelectron microscopy4.30i1-434[»]
5GAGelectron microscopy3.80i4-434[»]
5GAHelectron microscopy3.80i1-434[»]
ProteinModelPortaliP0AGD7.
SMRiP0AGD7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AGD7.

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 annotation2 Publications

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CB9. Bacteria.
COG0541. LUCA.
HOGENOMiHOG000036164.
InParanoidiP0AGD7.
KOiK03106.
OMAiMLPGMGQ.
PhylomeDBiP0AGD7.

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.

P0AGD7-1 [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 cautioni

The sequence CAA25957 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01818 Genomic DNA. Translation: CAA25957.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75659.1.
AP009048 Genomic DNA. Translation: BAA16495.2.
PIRiE65039.
RefSeqiNP_417101.1. NC_000913.3.
WP_000460035.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75659; AAC75659; b2610.
BAA16495; BAA16495; BAA16495.
GeneIDi947102.
KEGGiecj:JW5414.
eco:b2610.
PATRICi32120619. VBIEscCol129921_2708.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01818 Genomic DNA. Translation: CAA25957.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75659.1.
AP009048 Genomic DNA. Translation: BAA16495.2.
PIRiE65039.
RefSeqiNP_417101.1. NC_000913.3.
WP_000460035.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DULX-ray1.80A329-430[»]
1HQ1X-ray1.52A328-432[»]
2J28electron microscopy8.0092-431[»]
2PXBX-ray2.00A329-430[»]
2PXDX-ray2.00A329-430[»]
2PXEX-ray2.00A329-430[»]
2PXFX-ray2.00A329-430[»]
2PXKX-ray2.00A329-430[»]
2PXLX-ray2.50A329-430[»]
2PXPX-ray2.50A329-430[»]
2PXQX-ray2.50A329-430[»]
2PXTX-ray2.50A329-430[»]
2PXUX-ray2.50A329-430[»]
2PXVX-ray2.00A329-430[»]
2XKVelectron microscopy13.50C329-430[»]
2XXAX-ray3.94A/C1-433[»]
3LQXX-ray1.93A329-428[»]
4C7OX-ray2.60A/C1-298[»]
5AKAelectron microscopy5.705328-436[»]
5GADelectron microscopy3.70i4-434[»]
5GAFelectron microscopy4.30i1-434[»]
5GAGelectron microscopy3.80i4-434[»]
5GAHelectron microscopy3.80i1-434[»]
ProteinModelPortaliP0AGD7.
SMRiP0AGD7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262086. 262 interactors.
DIPiDIP-31865N.
IntActiP0AGD7. 19 interactors.
MINTiMINT-1218614.
STRINGi511145.b2610.

Protein family/group databases

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

Proteomic databases

EPDiP0AGD7.
PaxDbiP0AGD7.
PRIDEiP0AGD7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75659; AAC75659; b2610.
BAA16495; BAA16495; BAA16495.
GeneIDi947102.
KEGGiecj:JW5414.
eco:b2610.
PATRICi32120619. VBIEscCol129921_2708.

Organism-specific databases

EchoBASEiEB0296.
EcoGeneiEG10300. ffh.

Phylogenomic databases

eggNOGiENOG4105CB9. Bacteria.
COG0541. LUCA.
HOGENOMiHOG000036164.
InParanoidiP0AGD7.
KOiK03106.
OMAiMLPGMGQ.
PhylomeDBiP0AGD7.

Enzyme and pathway databases

BioCyciEcoCyc:EG10300-MONOMER.
ECOL316407:JW5414-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AGD7.
PROiP0AGD7.

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_ECOLI
AccessioniPrimary (citable) accession number: P0AGD7
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: November 30, 2016
This is version 111 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, 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.