O07347 (SRP54_THEAQ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Signal recognition particle protein

Alternative name(s):
Fifty-four homolog

Gene names

Name:

ffh

Organism

Thermus aquaticus

Taxonomic identifier

271 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	430 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity. HAMAP-Rule MF_00306
Subunit structure	Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY By similarity.
Subcellular location	Cytoplasm By similarity. Note: The SRP-RNC complex is targeted to the cytoplasmic membrane By similarity.
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.2 Ref.4 Ref.5
Sequence similarities	Belongs to the GTP-binding SRP family. SRP54 subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm Signal recognition particle
Ligand	GTP-binding Nucleotide-binding RNA-binding
Molecular function	Ribonucleoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC SRP-dependent cotranslational protein targeting to membrane Inferred from electronic annotation. Source: InterPro
Cellular_component	signal recognition particle, endoplasmic reticulum targeting Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	7S RNA binding Inferred from electronic annotation. Source: InterPro GTP binding Inferred from electronic annotation. Source: HAMAP GTPase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ftsY	P83749	2	EBI-1037906,EBI-1037899

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed HAMAP-Rule MF_00306

Chain

2 – 430

429

Signal recognition particle protein HAMAP-Rule MF_00306

PRO_0000101170

Regions

Nucleotide binding

105 – 112

8

GTP By similarity

Nucleotide binding

187 – 191

5

GTP By similarity

Nucleotide binding

245 – 248

4

GTP By similarity

Secondary structure

1

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430

Helix Strand Turn

Details...

Helix

3 – 14

12

Turn

15 – 18

4

Beta strand

19 – 21

3

Helix

24 – 40

17

Helix

45 – 61

17

Turn

62 – 66

5

Helix

70 – 85

16

Beta strand

97 – 104

8

Turn

107 – 110

4

Helix

111 – 124

14

Beta strand

129 – 133

5

Helix

139 – 152

14

Beta strand

156 – 158

3

Helix

165 – 179

15

Beta strand

183 – 187

5

Helix

196 – 209

14

Beta strand

212 – 219

8

Helix

220 – 223

4

Helix

224 – 236

13

Beta strand

241 – 245

5

Helix

247 – 249

3

Helix

254 – 263

10

Beta strand

267 – 270

4

Beta strand

273 – 275

3

Helix

276 – 278

3

Beta strand

279 – 281

3

Helix

284 – 291

8

Helix

300 – 306

7

Helix

322 – 334

13

Helix

341 – 343

3

Helix

356 – 367

12

Helix

371 – 375

5

Helix

377 – 379

3

Helix

382 – 392

11

Helix

396 – 415

20

Sequences

	Sequence		Length	Mass (Da)
	O07347 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 49F76AB5BC5D7D3F	FASTA	430	47,356
	10 20 30 40 50 60 MFQQLSARLQ EAIGRLRGRG RITEEDLKAT LREIRRALMD ADVNLEVARD FVERVREEAL 70 80 90 100 110 120 GKQVLESLTP AEVILATVYE ALKEALGGEA RLPVLKDRNL WFLVGLQGSG KTTTAAKLAL 130 140 150 160 170 180 YYKGKGRRPL LVAADTQRPA AREQLRLLGE KVGVPVLEVM DGESPESIRR RVEEKARLEA 190 200 210 220 230 240 RDLILVDTAG RLQIDEPLMG ELARLKEVLG PDEVLLVLDA MTGQEALSVA RAFDEKVGVT 250 260 270 280 290 300 GLVLTKLDGD ARGGAALSAR HVTGKPIYFA GVSEKPEGLE PFYPERLAGR ILGMGDVASL 310 320 330 340 350 360 AEKVRAAGLE AEAPKSAKEL SLEDFLKQMQ NLKRLGPFSE ILGLLPGVPQ GLKVDEKAIK 370 380 390 400 410 420 RLEAIVLSMT PEERKDPRIL NGSRRKRIAK GSGTSVQEVN RFIKAFEEMK ALMKSLEKKK 430 GRGLMGMFRR

References

[1]	Freymann D.M., Keenan R.J., Stroud R.M., Walter P. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Structure of the conserved GTPase domain of the signal recognition particle." Freymann D.M., Keenan R.J., Stroud R.M., Walter P. Nature 385:361-364(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-295, DOMAIN.
[3]	"Crystal structure of the signal sequence binding subunit of the signal recognition particle." Keenan R.J., Freymann D.M., Walter P., Stroud R.M. Cell 94:181-191(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
[4]	"Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP." Freymann D.M., Keenan R.J., Stroud R.M., Walter P. Nat. Struct. Biol. 6:793-801(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-295, DOMAIN.
[5]	"Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY." Shepotinovskaya I.V., Focia P.J., Freymann D.M. Acta Crystallogr. D 59:1834-1837(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CRYSTALLIZATION, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DOMAIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U82109 Genomic DNA. Translation: AAB58502.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFH	X-ray	2.05	A	2-295	[»]
1JPJ	X-ray	2.30	A	1-296	[»]
1JPN	X-ray	1.90	A/B	1-296	[»]
1LS1	X-ray	1.10	A	1-295	[»]
1NG1	X-ray	2.03	A	1-294	[»]
1O87	X-ray	2.10	A/B	1-297	[»]
1OKK	X-ray	2.05	A	1-294	[»]
1RJ9	X-ray	1.90	B	1-300	[»]
1RY1	electron microscopy	12.00	U	2-295	[»]
2C03	X-ray	1.24	A/B	2-296	[»]
2C04	X-ray	1.15	A/B	2-296	[»]
2CNW	X-ray	2.39	A/B/C	2-293	[»]
2FFH	X-ray	3.20	A/B/C	1-425	[»]
2IY3	electron microscopy	16.00	A	2-295	[»]
2J45	X-ray	1.14	A/B	2-296	[»]
2J46	X-ray	1.14	A/B	2-296	[»]
2J7P	X-ray	1.97	A/B	2-293	[»]
2NG1	X-ray	2.02	A	2-294	[»]
2XKV	electron microscopy	13.50	A	1-294	[»]
3NG1	X-ray	2.30	A/B	1-294	[»]
3ZN8	electron microscopy	12.00	A	2-295	[»]

ProteinModelPortal

O07347.

SMR

O07347. Positions 1-418.

ModBase

Search...

Protein-protein interaction databases

IntAct

O07347. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.260.30. 1 hit.

HAMAP

MF_00306. SRP54.

InterPro

IPR003593. AAA+_ATPase.
IPR013822. Signal_recog_particl_SRP54_hlx.
IPR004125. Signal_recog_particle_SRP54_M.
IPR022941. SRP54.
IPR000897. SRP54_GTPase_dom.
IPR004780. SRP_Ffh.
[Graphical view]

PANTHER

PTHR11564:SF7. PTHR11564:SF7. 1 hit.

Pfam

PF00448. SRP54. 1 hit.
PF02881. SRP54_N. 1 hit.
PF02978. SRP_SPB. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
SM00962. SRP54. 1 hit.
SM00963. SRP54_N. 1 hit.
[Graphical view]

SUPFAM

SSF47446. Signal_recog_particle_SRP54_M. 1 hit.
SSF47364. SRP54. 1 hit.

TIGRFAMs

TIGR00959. ffh. 1 hit.

PROSITE

PS00300. SRP54. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O07347.

Entry information

Entry name

SRP54_THEAQ

Accession

Primary (citable) accession number: O07347

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 85 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program