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Protein

Signal recognition particle protein

Gene

ffh

Organism
Thermus aquaticus
Status
Reviewed-Annotation score: Annotation score: 3 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.UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi105 – 1128GTPUniRule annotation
Nucleotide bindingi187 – 1915GTPUniRule annotation
Nucleotide bindingi245 – 2484GTPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

GTP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Signal recognition particle proteinUniRule annotation
Alternative name(s):
Fifty-four homologUniRule annotation
Gene namesi
Name:ffhUniRule annotation
OrganismiThermus aquaticus
Taxonomic identifieri271 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

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
Initiator methionineiRemoved
Chaini2 – 430429Signal recognition particle proteinPRO_0000101170Add
BLAST

Interactioni

Subunit structurei

Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
ftsYP837492EBI-1037906,EBI-1037899

Protein-protein interaction databases

IntActiO07347. 1 interaction.
STRINGi498848.TaqDRAFT_5389.

Structurei

Secondary structure

1
430
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1412Combined sources
Turni15 – 184Combined sources
Beta strandi19 – 213Combined sources
Helixi24 – 4017Combined sources
Helixi45 – 6117Combined sources
Turni62 – 665Combined sources
Helixi70 – 8516Combined sources
Beta strandi97 – 1048Combined sources
Turni107 – 1104Combined sources
Helixi111 – 12414Combined sources
Beta strandi129 – 1335Combined sources
Helixi139 – 15214Combined sources
Beta strandi156 – 1583Combined sources
Helixi165 – 17915Combined sources
Beta strandi183 – 1875Combined sources
Helixi196 – 20914Combined sources
Beta strandi212 – 2198Combined sources
Helixi220 – 2234Combined sources
Helixi224 – 23613Combined sources
Beta strandi241 – 2455Combined sources
Helixi247 – 2493Combined sources
Helixi254 – 26310Combined sources
Beta strandi267 – 2704Combined sources
Beta strandi273 – 2753Combined sources
Helixi276 – 2783Combined sources
Beta strandi279 – 2813Combined sources
Helixi284 – 2918Combined sources
Helixi300 – 3067Combined sources
Helixi322 – 33413Combined sources
Helixi341 – 3433Combined sources
Helixi356 – 36712Combined sources
Helixi371 – 3755Combined sources
Helixi377 – 3793Combined sources
Helixi382 – 39211Combined sources
Helixi396 – 41520Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFHX-ray2.05A2-295[»]
1JPJX-ray2.30A1-296[»]
1JPNX-ray1.90A/B1-296[»]
1LS1X-ray1.10A1-295[»]
1NG1X-ray2.03A1-294[»]
1O87X-ray2.10A/B2-297[»]
1OKKX-ray2.05A1-294[»]
1RJ9X-ray1.90B1-300[»]
1RY1electron microscopy12.00U1-296[»]
2C03X-ray1.24A/B2-297[»]
2C04X-ray1.15A/B2-297[»]
2CNWX-ray2.39A/B/C2-294[»]
2FFHX-ray3.20A/B/C1-425[»]
2IY3electron microscopy16.00A2-296[»]
2J45X-ray1.14A/B2-297[»]
2J46X-ray1.14A/B2-297[»]
2J7PX-ray1.97A/B2-294[»]
2NG1X-ray2.02A2-294[»]
2XKVelectron microscopy13.50A1-294[»]
3NG1X-ray2.30A/B1-294[»]
3ZN8electron microscopy12.00A2-295[»]
ProteinModelPortaliO07347.
SMRiO07347. Positions 1-418.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO07347.

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 annotation3 Publications

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CB9. Bacteria.
COG0541. LUCA.

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]
SUPFAMiSSF47364. SSF47364. 1 hit.
SSF47446. SSF47446. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00959. ffh. 1 hit.
PROSITEiPS00300. SRP54. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O07347-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFQQLSARLQ EAIGRLRGRG RITEEDLKAT LREIRRALMD ADVNLEVARD
60 70 80 90 100
FVERVREEAL GKQVLESLTP AEVILATVYE ALKEALGGEA RLPVLKDRNL
110 120 130 140 150
WFLVGLQGSG KTTTAAKLAL YYKGKGRRPL LVAADTQRPA AREQLRLLGE
160 170 180 190 200
KVGVPVLEVM DGESPESIRR RVEEKARLEA RDLILVDTAG RLQIDEPLMG
210 220 230 240 250
ELARLKEVLG PDEVLLVLDA MTGQEALSVA RAFDEKVGVT GLVLTKLDGD
260 270 280 290 300
ARGGAALSAR HVTGKPIYFA GVSEKPEGLE PFYPERLAGR ILGMGDVASL
310 320 330 340 350
AEKVRAAGLE AEAPKSAKEL SLEDFLKQMQ NLKRLGPFSE ILGLLPGVPQ
360 370 380 390 400
GLKVDEKAIK RLEAIVLSMT PEERKDPRIL NGSRRKRIAK GSGTSVQEVN
410 420 430
RFIKAFEEMK ALMKSLEKKK GRGLMGMFRR
Length:430
Mass (Da):47,356
Last modified:January 23, 2007 - v3
Checksum:i49F76AB5BC5D7D3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82109 Genomic DNA. Translation: AAB58502.1.
RefSeqiWP_003045728.1. NZ_LHCI01000106.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82109 Genomic DNA. Translation: AAB58502.1.
RefSeqiWP_003045728.1. NZ_LHCI01000106.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFHX-ray2.05A2-295[»]
1JPJX-ray2.30A1-296[»]
1JPNX-ray1.90A/B1-296[»]
1LS1X-ray1.10A1-295[»]
1NG1X-ray2.03A1-294[»]
1O87X-ray2.10A/B2-297[»]
1OKKX-ray2.05A1-294[»]
1RJ9X-ray1.90B1-300[»]
1RY1electron microscopy12.00U1-296[»]
2C03X-ray1.24A/B2-297[»]
2C04X-ray1.15A/B2-297[»]
2CNWX-ray2.39A/B/C2-294[»]
2FFHX-ray3.20A/B/C1-425[»]
2IY3electron microscopy16.00A2-296[»]
2J45X-ray1.14A/B2-297[»]
2J46X-ray1.14A/B2-297[»]
2J7PX-ray1.97A/B2-294[»]
2NG1X-ray2.02A2-294[»]
2XKVelectron microscopy13.50A1-294[»]
3NG1X-ray2.30A/B1-294[»]
3ZN8electron microscopy12.00A2-295[»]
ProteinModelPortaliO07347.
SMRiO07347. Positions 1-418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO07347. 1 interaction.
STRINGi498848.TaqDRAFT_5389.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CB9. Bacteria.
COG0541. LUCA.

Miscellaneous databases

EvolutionaryTraceiO07347.

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]
SUPFAMiSSF47364. SSF47364. 1 hit.
SSF47446. SSF47446. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00959. ffh. 1 hit.
PROSITEiPS00300. SRP54. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSRP54_THEAQ
AccessioniPrimary (citable) accession number: O07347
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.