P37107 (SR54C_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Signal recognition particle 54 kDa protein, chloroplastic
Short name=54 chloroplast protein
Short name=54CP
Short name=SRP54
Short name=cpSRP54

Alternative name(s):
FFC

Gene names

Name:	FFC
Synonyms:	CPSRP54
Ordered Locus Names:	At5g03940
ORF Names:	F8F6_150

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	564 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 cotranslational and post-translational sorting of thylakoid proteins. Binds GTP specifically. Activates the GTPase activity of CPFTSY when bound together. Required for light-harvesting chlorophyll a/b-binding protein (LHCP) integration into thylakoids. Ref.7 Ref.8 Ref.11 Ref.12
Subunit structure	Component of the cpSRP complex, composed of a FFC/cpSRP54 monomer and a CAO/cpSRP43 dimer. Interacts (via C-terminus) with CAO/cpSRP43 and with CPFTSY. Interacts with the third transmembrane domain of LHCP. Interacts with the PSBA/D1 nascent chain, but only when it is attached to the 70S ribosome and if it is shorter than 189 amino acid residues. Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.13
Subcellular location	Plastid › chloroplast stroma.
Tissue specificity	Most abundant in green shoot tissue and lower levels seen in the roots and etiolated buds. Ref.10
Domain	The M-domain stimulates the interaction between CPFTSY and the chloroplast signal recogniton particle (cpSRP). The C-terminal residues (539-564) are required for interaction with CAO/cpSRP43.
Disruption phenotype	Pale green with delayed development. Ref.12
Miscellaneous	Unlike eukaryotic or prokaryotic signal recognition particle (SRP), the chloroplast SRP from higher plants lacks an SRP-RNA component. It targets both chloroplast-encoded and nucleus-encoded substrates to the thylakoid membrane, post-translationally for the nucleus-encoded proteins and co-translationally for the chloroplast-encoded proteins.
Sequence similarities	Belongs to the GTP-binding SRP family.

Ontologies

Keywords
Cellular component	Chloroplast Plastid Signal recognition particle
Domain	Transit peptide
Ligand	GTP-binding Nucleotide-binding RNA-binding
Molecular function	Ribonucleoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	SRP-dependent cotranslational protein targeting to membrane Inferred from electronic annotation. Source: InterPro
Cellular component	chloroplast stroma Inferred from direct assay. Source: TAIR signal recognition particle, chloroplast targeting Inferred from mutant phenotype. Source: TAIR 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: UniProtKB-KW nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CAO	O22265	9	EBI-780642,EBI-780656

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 75

75

Chloroplast

Chain

76 – 564

489

Signal recognition particle 54 kDa protein, chloroplastic

PRO_0000033232

Regions

Nucleotide binding

183 – 190

8

GTP By similarity

Nucleotide binding

265 – 269

5

GTP By similarity

Nucleotide binding

323 – 326

4

GTP By similarity

Region

76 – 370

295

G-domain

Region

371 – 564

194

M-domain

Experimental info

Mutagenesis

536

1

R → G or K: Strongly reduced binding to CAO/cpSRP43. Ref.9

Mutagenesis

537

1

R → G, Q, K or N: Loss of binding to CAO/cpSRP43. Ref.9

Mutagenesis

538 – 540

3

Missing: No effect on binding to CAO/cpSRP43. Ref.9

Mutagenesis

538

1

K → M: No effect on binding to CAO/cpSRP43. Ref.9

Mutagenesis

539

1

R → G or K: Reduced binding to CAO/cpSRP43. Ref.9

Mutagenesis

540

1

K → M: No effect on binding to CAO/cpSRP43. Ref.9

Sequence conflict

76

1

E → V in AAC64139. Ref.2

Secondary structure

1

.

.

.

564

Helix Strand Turn

Details...

Beta strand

537 – 539

3

Sequences

	Sequence		Length	Mass (Da)
	P37107 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 423F7285FB9063E4	FASTA	564	61,232
	10 20 30 40 50 60 MEALQFSSVN RVPCTLSCTG NRRIKAAFSS AFTGGTINSA SLSSSRNLST REIWSWVKSK 70 80 90 100 110 120 TVVGHGRYRR SQVRAEMFGQ LTGGLEAAWS KLKGEEVLTK DNIAEPMRDI RRALLEADVS 130 140 150 160 170 180 LPVVRRFVQS VSDQAVGMGV IRGVKPDQQL VKIVHDELVK LMGGEVSELQ FAKSGPTVIL 190 200 210 220 230 240 LAGLQGVGKT TVCAKLACYL KKQGKSCMLI AGDVYRPAAI DQLVILGEQV GVPVYTAGTD 250 260 270 280 290 300 VKPADIAKQG LKEAKKNNVD VVIMDTAGRL QIDKGMMDEL KDVKKFLNPT EVLLVVDAMT 310 320 330 340 350 360 GQEAAALVTT FNVEIGITGA ILTKLDGDSR GGAALSVKEV SGKPIKLVGR GERMEDLEPF 370 380 390 400 410 420 YPDRMAGRIL GMGDVLSFVE KATEVMRQED AEDLQKKIMS AKFDFNDFLK QTRAVAKMGS 430 440 450 460 470 480 MTRVLGMIPG MGKVSPAQIR EAEKNLLVME AMIEVMTPEE RERPELLAES PERRKRIAKD 490 500 510 520 530 540 SGKTEQQVSA LVAQIFQMRV KMKNLMGVME GGSIPALSGL EDALKAEQKA PPGTARRKRK 550 560 ADSRKKFVES ASSKPGPRGF GSGN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a chloroplast homologue of the 54-kDa subunit of the signal recognition particle." Franklin A.E., Hoffman N.E. J. Biol. Chem. 268:22175-22180(1993) [PubMed: 8408079] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Isolation of two Arabidopsis mutants in the nuclear gene ffc, encoding the 54 kDa subunit of chloroplast signal recognition particle." Amin P., Sy D., Pilgrim M., Parry D.H., Hoffman N.E. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Interactions of ribosome nascent chain complexes of the chloroplast-encoded D1 thylakoid membrane protein with cpSRP54." Nilsson R., Brunner J., Hoffman N.E., van Wijk K.J. EMBO J. 18:733-742(1999) [PubMed: 9927433] [Abstract] Cited for: INTERACTION WITH PSBA.
[7]	"Chloroplast FtsY, chloroplast signal recognition particle, and GTP are required to reconstitute the soluble phase of light-harvesting chlorophyll protein transport into thylakoid membranes." Tu C.J., Schuenemann D., Hoffman N.E. J. Biol. Chem. 274:27219-27224(1999) [PubMed: 10480939] [Abstract] Cited for: FUNCTION, INTERACTION WITH CAO/CPSRP43.
[8]	"Functional characterization of recombinant chloroplast signal recognition particle." Groves M.R., Mant A., Kuhn A., Koch J., Duebel S., Robinson C., Sinning I. J. Biol. Chem. 276:27778-27786(2001) [PubMed: 11356852] [Abstract] Cited for: FUNCTION, INTERACTION WITH CAO/CPSRP43 AND LHCP.
[9]	"A unique sequence motif in the 54-kDa subunit of the chloroplast signal recognition particle mediates binding to the 43-kDa subunit." Funke S., Knechten T., Ollesch J., Schunemann D. J. Biol. Chem. 280:8912-8917(2005) [PubMed: 15632183] [Abstract] Cited for: INTERACTION WITH CAO/CPSRP43, MUTAGENESIS OF ARG-536; ARG-537; LYS-538; ARG-539 AND LYS-540.
[10]	"Arabidopsis cpFtsY mutants exhibit pleiotropic defects including an inability to increase iron deficiency-inducible root Fe(III) chelate reductase activity." Durrett T.P., Connolly E.L., Rogers E.E. Plant J. 47:467-479(2006) [PubMed: 16813577] [Abstract] Cited for: TISSUE SPECIFICITY.
[11]	"Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA." Jaru-Ampornpan P., Chandrasekar S., Shan S.O. Mol. Biol. Cell 18:2636-2645(2007) [PubMed: 17475780] [Abstract] Cited for: FUNCTION, INTERACTION WITH CPFTSY.
[12]	"Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis." Rutschow H., Ytterberg A.J., Friso G., Nilsson R., van Wijk K.J. Plant Physiol. 148:156-175(2008) [PubMed: 18633119] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[13]	"A distinct mechanism to achieve efficient signal recognition particle (SRP)-SRP receptor interaction by the chloroplast srp pathway." Jaru-Ampornpan P., Nguyen T.X., Shan S.O. Mol. Biol. Cell 20:3965-3973(2009) [PubMed: 19587121] [Abstract] Cited for: INTERACTION WITH CPFTSY.
[14]	"Assembly of chloroplast signal recognition particle involves structural rearrangement in cpSRP43." Kathir K.M., Rajalingam D., Sivaraja V., Kight A., Goforth R.L., Yu C., Henry R., Kumar T.K. J. Mol. Biol. 381:49-60(2008) [PubMed: 18586266] [Abstract] Cited for: STRUCTURE BY NMR OF 530-543.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z21970 mRNA. Translation: CAA79981.1.
AF092168 Genomic DNA. Translation: AAC64139.1.
AL162873 Genomic DNA. Translation: CAB85514.1.
CP002688 Genomic DNA. Translation: AED90674.1.
AY050999 mRNA. Translation: AAK93676.1.
BT000976 mRNA. Translation: AAN41376.1.

IPI

IPI00538977.

PIR

S36637.

RefSeq

NP_196014.1. NM_120476.4.

UniGene

At.435.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HUG	NMR	-	B	530-543	[»]

ProteinModelPortal

P37107.

SMR

P37107. Positions 78-561.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-752N.

IntAct

P37107. 4 interactions.

MINT

MINT-126488.

STRING

P37107.

Protein family/group databases

TCDB

3.A.5.1.2. general secretory pathway (Sec) family.

Proteomic databases

PRIDE

P37107.

ProMEX

P37107.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT5G03940.1; AT5G03940.1; AT5G03940.

GeneID

830273.

GenomeReviews

Gene locus AT5G03940 in contig BA000015_GR.

KEGG

ath:AT5G03940.

NMPDR

fig|3702.1.peg.22486.

Organism-specific databases

GeneFarm

1888. 217.

TAIR

At5g03940.

Phylogenomic databases

eggNOG

KOG0780.

GeneTree

EPGT00070000029738.

HOGENOM

HBG562580.

InParanoid

P37107.

OMA

NVEIGIT.

PhylomeDB

P37107.

ProtClustDB

CLSN2686225.

Gene expression databases

ArrayExpress

P37107.

Genevestigator

P37107.

GermOnline

AT5G03940. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR003593. ATPase_AAA+_core.
IPR000897. Signal_recog_part_SRP54_GTPase.
IPR013822. Signal_recog_particl_SRP54_hlx.
IPR004780. Signal_recog_particle_SRP.
IPR004125. Signal_recog_particle_SRP54_M.
[Graphical view]

Gene3D

G3DSA:1.20.120.140. SRP54_helical. 1 hit.
G3DSA:1.10.260.30. SRP54_M. 1 hit.

KO

K03106.

PANTHER

PTHR11564:SF7. SRP_sub. 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...

Entry information

Entry name

SR54C_ARATH

Accession

Primary (citable) accession number: P37107
Secondary accession number(s): O82570

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	January 25, 2012
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program