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UniProtKB - P0AGD7 (SRP54_ECOLI)

UniProt

P0AGD7 - SRP54_ECOLI

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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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi107 – 1148GTPUniRule annotation
Nucleotide bindingi190 – 1945GTPUniRule annotation
Nucleotide bindingi248 – 2514GTPUniRule annotation

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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453Signal recognition particle proteinPRO_0000101153Add
BLAST

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 interactions.
DIPiDIP-31865N.
IntActiP0AGD7. 19 interactions.
MINTiMINT-1218614.
STRINGi511145.b2610.

Structurei

Secondary structure

1
453
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1511Combined sources
Helixi24 – 4017Combined sources
Helixi45 – 6016Combined sources
Helixi70 – 8617Combined sources
Beta strandi96 – 10611Combined sources
Helixi113 – 12614Combined sources
Beta strandi132 – 1365Combined sources
Helixi144 – 15512Combined sources
Beta strandi158 – 1603Combined sources
Helixi168 – 18114Combined sources
Beta strandi185 – 1906Combined sources
Helixi199 – 21214Combined sources
Beta strandi215 – 2228Combined sources
Helixi229 – 23911Combined sources
Beta strandi244 – 2485Combined sources
Helixi258 – 2669Combined sources
Beta strandi270 – 2745Combined sources
Beta strandi276 – 2783Combined sources
Beta strandi282 – 2843Combined sources
Helixi287 – 2959Combined sources
Helixi331 – 3388Combined sources
Helixi373 – 3819Combined sources
Helixi385 – 3895Combined sources
Helixi391 – 3933Combined sources
Helixi396 – 40510Combined sources
Helixi410 – 43021Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-431.
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
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. Positions 2-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262086. 262 interactions.
DIPiDIP-31865N.
IntActiP0AGD7. 19 interactions.
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: September 7, 2016
This is version 108 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.