UniProtKB - P0AGD7 (SRP54_ECOLI)
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Protein
Signal recognition particle protein
Gene
ffh
Organism
Escherichia coli (strain K12)
Status
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 107 – 114 | GTPUniRule annotation | 8 | |
Nucleotide bindingi | 190 – 194 | GTPUniRule annotation | 5 | |
Nucleotide bindingi | 248 – 251 | GTPUniRule annotation | 4 |
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
Keywordsi
Molecular function | Ribonucleoprotein, RNA-binding |
Ligand | GTP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10300-MONOMER. |
Protein family/group databases
TCDBi | 3.A.5.1.1. the general secretory pathway (sec) family. |
Names & Taxonomyi
Protein namesi | Recommended name: Signal recognition particle proteinUniRule annotationAlternative name(s): Fifty-four homologUniRule annotation Short name: Ffh p48 |
Gene namesi | Name:ffhUniRule annotation Ordered Locus Names:b2610, JW5414 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Organism-specific databases
EcoGenei | EG10300. 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
Keywords - Cellular componenti
Cytoplasm, Signal recognition particlePathology & 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000101153 | 1 – 453 | Signal recognition particle proteinAdd BLAST | 453 |
Proteomic databases
EPDi | P0AGD7. |
PaxDbi | P0AGD7. |
PRIDEi | P0AGD7. |
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
Binary interactionsi
Protein-protein interaction databases
BioGridi | 4262086. 316 interactors. |
DIPi | DIP-31865N. |
IntActi | P0AGD7. 22 interactors. |
STRINGi | 316385.ECDH10B_2777. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Helixi | 5 – 15 | Combined sources | 11 | |
Helixi | 24 – 40 | Combined sources | 17 | |
Helixi | 45 – 60 | Combined sources | 16 | |
Helixi | 70 – 86 | Combined sources | 17 | |
Beta strandi | 96 – 106 | Combined sources | 11 | |
Helixi | 113 – 126 | Combined sources | 14 | |
Beta strandi | 132 – 136 | Combined sources | 5 | |
Helixi | 144 – 155 | Combined sources | 12 | |
Beta strandi | 158 – 160 | Combined sources | 3 | |
Helixi | 168 – 181 | Combined sources | 14 | |
Beta strandi | 185 – 190 | Combined sources | 6 | |
Helixi | 199 – 212 | Combined sources | 14 | |
Beta strandi | 215 – 222 | Combined sources | 8 | |
Helixi | 229 – 239 | Combined sources | 11 | |
Beta strandi | 244 – 248 | Combined sources | 5 | |
Helixi | 258 – 266 | Combined sources | 9 | |
Beta strandi | 270 – 274 | Combined sources | 5 | |
Beta strandi | 276 – 278 | Combined sources | 3 | |
Beta strandi | 282 – 284 | Combined sources | 3 | |
Helixi | 287 – 295 | Combined sources | 9 | |
Helixi | 331 – 338 | Combined sources | 8 | |
Helixi | 373 – 381 | Combined sources | 9 | |
Helixi | 385 – 389 | Combined sources | 5 | |
Helixi | 391 – 393 | Combined sources | 3 | |
Helixi | 396 – 405 | Combined sources | 10 | |
Helixi | 410 – 430 | Combined sources | 21 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1DUL | X-ray | 1.80 | A | 371-430 | [»] | |
1HQ1 | X-ray | 1.52 | A | 328-432 | [»] | |
2J28 | electron microscopy | 8.00 | 9 | 2-431 | [»] | |
2PXB | X-ray | 2.00 | A | 329-430 | [»] | |
2PXD | X-ray | 2.00 | A | 329-430 | [»] | |
2PXE | X-ray | 2.00 | A | 329-430 | [»] | |
2PXF | X-ray | 2.00 | A | 329-430 | [»] | |
2PXK | X-ray | 2.00 | A | 329-430 | [»] | |
2PXL | X-ray | 2.50 | A | 329-430 | [»] | |
2PXP | X-ray | 2.50 | A | 329-430 | [»] | |
2PXQ | X-ray | 2.50 | A | 329-430 | [»] | |
2PXT | X-ray | 2.50 | A | 329-430 | [»] | |
2PXU | X-ray | 2.50 | A | 329-430 | [»] | |
2PXV | X-ray | 2.00 | A | 329-430 | [»] | |
2XKV | electron microscopy | 13.50 | C | 371-430 | [»] | |
2XXA | X-ray | 3.94 | A/C | 1-433 | [»] | |
3LQX | X-ray | 1.93 | A | 329-428 | [»] | |
4C7O | X-ray | 2.60 | A/C | 1-298 | [»] | |
5AKA | electron microscopy | 5.70 | 5 | 328-436 | [»] | |
5GAD | electron microscopy | 3.70 | i | 4-434 | [»] | |
5GAF | electron microscopy | 4.30 | i | 1-434 | [»] | |
5GAG | electron microscopy | 3.80 | i | 4-434 | [»] | |
5GAH | electron microscopy | 3.80 | i | 1-434 | [»] | |
5NCO | electron microscopy | 4.80 | i | 4-434 | [»] | |
ProteinModelPortali | P0AGD7. | |||||
SMRi | P0AGD7. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0AGD7. |
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
Phylogenomic databases
eggNOGi | ENOG4105CB9. Bacteria. COG0541. LUCA. |
HOGENOMi | HOG000036164. |
InParanoidi | P0AGD7. |
KOi | K03106. |
OMAi | DTAGRHK. |
PhylomeDBi | P0AGD7. |
Family and domain databases
Gene3Di | 1.10.260.30. 1 hit. |
HAMAPi | MF_00306. SRP54. 1 hit. |
InterProi | View protein in InterPro IPR003593. AAA+_ATPase. IPR027417. P-loop_NTPase. IPR036891. Signal_recog_part_SRP54_M_sf. IPR013822. Signal_recog_particl_SRP54_hlx. IPR004125. Signal_recog_particle_SRP54_M. IPR022941. SRP54. IPR000897. SRP54_GTPase_dom. IPR004780. SRP_Ffh. |
PANTHERi | PTHR11564. PTHR11564. 1 hit. PTHR11564:SF7. PTHR11564:SF7. 1 hit. |
Pfami | View protein in Pfam PF00448. SRP54. 1 hit. PF02881. SRP54_N. 1 hit. PF02978. SRP_SPB. 1 hit. |
SMARTi | View protein in SMART SM00382. AAA. 1 hit. SM00962. SRP54. 1 hit. SM00963. SRP54_N. 1 hit. |
SUPFAMi | SSF47446. SSF47446. 1 hit. SSF52540. SSF52540. 1 hit. |
TIGRFAMsi | TIGR00959. ffh. 1 hit. |
PROSITEi | View protein in PROSITE PS00300. SRP54. 1 hit. |
i Sequence
Sequence statusi: Complete.
P0AGD7-1 [UniParc]FASTAAdd to basket
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
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. |
PIRi | E65039. |
RefSeqi | NP_417101.1. NC_000913.3. WP_000460035.1. NZ_LN832404.1. |
Genome annotation databases
EnsemblBacteriai | AAC75659; AAC75659; b2610. BAA16495; BAA16495; BAA16495. |
GeneIDi | 947102. |
KEGGi | ecj:JW5414. eco:b2610. |
PATRICi | fig|1411691.4.peg.4129. |
Similar proteinsi
Entry informationi
Entry namei | SRP54_ECOLI | |
Accessioni | P0AGD7Primary (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: | March 28, 2018 | |
This is version 124 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |