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P0AGD7 (SRP54_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal recognition particle protein
Alternative name(s):
Fifty-four homolog
Short name=Ffh
p48
Gene names
Name:ffh
Ordered Locus Names:b2610, JW5414
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.13

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.9

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. Metal ions are essential for the formation and stability of the SRP complex. Interacts with the ribosomes, via ribosomal protein L23. Interacts with FtsY. Ref.6 Ref.7 Ref.8 Ref.11 Ref.12 Ref.18

Subcellular location

Cytoplasm. Note: The SRP-RNC complex is targeted to the cytoplasmic membrane. HAMAP-Rule MF_00306

Domain

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. Ref.12 Ref.17

Disruption phenotype

Essential; deletion experiments lead to loss of inner membrane protein targeting. Also leads to reduced targeting of lipoproteins Lpp and BRP. Ref.10 Ref.13

Sequence similarities

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

Sequence caution

The sequence CAA25957.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 453453Signal recognition particle protein HAMAP-Rule MF_00306
PRO_0000101153

Regions

Nucleotide binding107 – 1148GTP By similarity
Nucleotide binding190 – 1945GTP By similarity
Nucleotide binding248 – 2514GTP By similarity

Secondary structure

..................................................... 453
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AGD7 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: E9C7A7101CC04D66

FASTA45349,787
        10         20         30         40         50         60 
MFDNLTDRLS RTLRNISGRG RLTEDNVKDT LREVRMALLE ADVALPVVRE FINRVKEKAV 

        70         80         90        100        110        120 
GHEVNKSLTP GQEFVKIVRN ELVAAMGEEN QTLNLAAQPP AVVLMAGLQG AGKTTSVGKL 

       130        140        150        160        170        180 
GKFLREKHKK KVLVVSADVY RPAAIKQLET LAEQVGVDFF PSDVGQKPVD IVNAALKEAK 

       190        200        210        220        230        240 
LKFYDVLLVD TAGRLHVDEA MMDEIKQVHA SINPVETLFV VDAMTGQDAA NTAKAFNEAL 

       250        260        270        280        290        300 
PLTGVVLTKV DGDARGGAAL SIRHITGKPI KFLGVGEKTE ALEPFHPDRI ASRILGMGDV 

       310        320        330        340        350        360 
LSLIEDIESK VDRAQAEKLA SKLKKGDGFD LNDFLEQLRQ MKNMGGMASL MGKLPGMGQI 

       370        380        390        400        410        420 
PDNVKSQMDD KVLVRMEAII NSMTMKERAK PEIIKGSRKR RIAAGCGMQV QDVNRLLKQF 

       430        440        450 
DDMQRMMKKM KKGGMAKMMR SMKGMMPPGF PGR 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of an Escherichia coli operon containing genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a 21-K polypeptide."
Bystroem A.S., Hjalmarsson K.J., Wikstroem P.M., Bjoerk G.R.
EMBO J. 2:899-905(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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 277:1453-1462(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], SEQUENCE REVISION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"E. coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle."
Ribes V., Roemisch K., Giner A., Dobberstein B., Tollervey D.
Cell 63:591-600(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex."
Luirink J., High S., Wood H., Giner A., Tollervey D., Dobberstein B.
Nature 359:741-743(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[7]"The E. coli ffh gene is necessary for viability and efficient protein export."
Phillips G.J., Silhavy T.J.
Nature 359:744-746(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[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.
[9]"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.
[10]"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.
[11]"Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome."
Ullers R.S., Houben E.N.G., Raine A., ten Hagen-Jongman C.M., Ehrenberg M., Brunner J., Oudega B., Harms N., Luirink J.
J. Cell Biol. 161:679-684(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RIBOSOMAL PROTEIN L23 AND NASCENT PROTEIN CHAINS.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[12]"The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome."
Gu S.-Q., Peske F., Wieden H.-J., Rodnina M.V., Wintermeyer W.
RNA 9:566-573(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RIBOSOMAL PROTEIN L23, DOMAIN.
Strain: MRE-600.
[13]"Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway."
Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W.
J. Biol. Chem. 279:31026-31032(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN LIPOPROTEIN EXPORT, DISRUPTION PHENOTYPE.
[14]"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: SIMULTANEOUS BINDING OF TRIGGER FACTOR AND SRP TO THE RIBOSOME.
Strain: MRE-600.
[15]"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.
[16]"Structure of a methionine-rich segment of Escherichia coli Ffh protein."
Oh D.-B., Yi G.-S., Chi S.-W., Kim H.
FEBS Lett. 395:160-164(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 410-434.
[17]"Crystal structure of the ribonucleoprotein core of the signal recognition particle."
Batey R.T., Rambo R.P., Lucast L., Rha B., Doudna J.A.
Science 287:1232-1239(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 371-430 IN COMPLEX WITH 4.5S RNA, DOMAIN.
[18]"Structural and energetic analysis of metal ions essential to SRP signal recognition domain assembly."
Batey R.T., Doudna J.A.
Biochemistry 41:11703-11710(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 328-432, SUBUNIT.
[19]"Following the signal sequence from ribosomal tunnel exit to signal recognition particle."
Halic M., Blau M., Becker T., Mielke T., Pool M.R., Wild K., Sinning I., Beckmann R.
Nature 444:507-511(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (8.00 ANGSTROMS) OF 2-431.
[20]"A general strategy to solve the phase problem in RNA crystallography."
Keel A.Y., Rambo R.P., Batey R.T., Kieft J.S.
Structure 15:761-772(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 329-430.
[21]"Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor."
Estrozi L.F., Boehringer D., Shan S.O., Ban N., Schaffitzel C.
Nat. Struct. Mol. Biol. 18:88-90(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (13.50 ANGSTROMS) OF 371-430.
[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 1-433.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01818 Genomic DNA. Translation: CAA25957.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75659.1.
AP009048 Genomic DNA. Translation: BAA16495.2.
PIRE65039.
RefSeqNP_417101.1. NC_000913.3.
YP_490833.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP0AGD7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31865N.
IntActP0AGD7. 19 interactions.
MINTMINT-1218614.
STRING511145.b2610.

Protein family/group databases

TCDB3.A.5.1.1. the general secretory pathway (sec) family.

Proteomic databases

PaxDbP0AGD7.
PRIDEP0AGD7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75659; AAC75659; b2610.
BAA16495; BAA16495; BAA16495.
GeneID12933092.
947102.
KEGGecj:Y75_p2558.
eco:b2610.
PATRIC32120619. VBIEscCol129921_2708.

Organism-specific databases

EchoBASEEB0296.
EcoGeneEG10300. ffh.

Phylogenomic databases

eggNOGCOG0541.
HOGENOMHOG000036164.
KOK03106.
OMALKQHKQM.
OrthoDBEOG62K1ZH.
PhylomeDBP0AGD7.

Enzyme and pathway databases

BioCycEcoCyc:EG10300-MONOMER.
ECOL316407:JW5414-MONOMER.

Gene expression databases

GenevestigatorP0AGD7.

Family and domain databases

Gene3D1.10.260.30. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_00306. SRP54.
InterProIPR003593. 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]
PANTHERPTHR11564:SF7. PTHR11564:SF7. 1 hit.
PfamPF00448. SRP54. 1 hit.
PF02881. SRP54_N. 1 hit.
PF02978. SRP_SPB. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM00962. SRP54. 1 hit.
SM00963. SRP54_N. 1 hit.
[Graphical view]
SUPFAMSSF47446. SSF47446. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00959. ffh. 1 hit.
PROSITEPS00300. SRP54. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AGD7.
PROP0AGD7.

Entry information

Entry nameSRP54_ECOLI
AccessionPrimary (citable) accession number: P0AGD7
Secondary accession number(s): P07019, P77007, P77008
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: December 20, 2005
Last modified: July 9, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene