Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Signal recognition particle 54 kDa protein, chloroplastic

Gene

FFC

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi183 – 1908GTPBy similarity
Nucleotide bindingi265 – 2695GTPBy similarity
Nucleotide bindingi323 – 3264GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

GTP-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

TCDBi3.A.5.1.2. the general secretory pathway (sec) family.

Names & Taxonomyi

Protein namesi
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 namesi
Name:FFC
Synonyms:CPSRP54
Ordered Locus Names:At5g03940
ORF Names:F8F6_150
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G03940.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • signal recognition particle, chloroplast targeting Source: TAIR
  • signal recognition particle, endoplasmic reticulum targeting Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid, Signal recognition particle

Pathology & Biotechi

Disruption phenotypei

Pale green with delayed development.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi536 – 5361R → G or K: Strongly reduced binding to CAO/cpSRP43. 1 Publication
Mutagenesisi537 – 5371R → G, Q, K or N: Loss of binding to CAO/cpSRP43. 1 Publication
Mutagenesisi538 – 5403Missing : No effect on binding to CAO/cpSRP43.
Mutagenesisi538 – 5381K → M: No effect on binding to CAO/cpSRP43. 1 Publication
Mutagenesisi539 – 5391R → G or K: Reduced binding to CAO/cpSRP43. 1 Publication
Mutagenesisi540 – 5401K → M: No effect on binding to CAO/cpSRP43. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7575ChloroplastAdd
BLAST
Chaini76 – 564489Signal recognition particle 54 kDa protein, chloroplasticPRO_0000033232Add
BLAST

Proteomic databases

PaxDbiP37107.
PRIDEiP37107.

Expressioni

Tissue specificityi

Most abundant in green shoot tissue and lower levels seen in the roots and etiolated buds.1 Publication

Gene expression databases

GenevisibleiP37107. AT.

Interactioni

Subunit structurei

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CAOO2226516EBI-780642,EBI-780656

Protein-protein interaction databases

BioGridi15553. 4 interactions.
DIPiDIP-752N.
IntActiP37107. 4 interactions.
MINTiMINT-126488.
STRINGi3702.AT5G03940.1.

Structurei

Secondary structure

1
564
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi534 – 5385Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HUGNMR-B530-543[»]
3UI2X-ray3.18B528-540[»]
ProteinModelPortaliP37107.
SMRiP37107. Positions 78-505.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37107.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni76 – 370295G-domainAdd
BLAST
Regioni371 – 564194M-domainAdd
BLAST

Domaini

The M-domain stimulates the interaction between CPFTSY and the chloroplast signal recognition particle (cpSRP).
The C-terminal residues (539-564) are required for interaction with CAO/cpSRP43.

Sequence similaritiesi

Belongs to the GTP-binding SRP family. SRP54 subfamily.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0780. Eukaryota.
COG0541. LUCA.
HOGENOMiHOG000036164.
InParanoidiP37107.
KOiK03106.
OMAiMQKLMGM.
PhylomeDBiP37107.

Family and domain databases

Gene3Di1.10.260.30. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00306. SRP54.
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]
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.

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

P37107-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEALQFSSVN RVPCTLSCTG NRRIKAAFSS AFTGGTINSA SLSSSRNLST
60 70 80 90 100
REIWSWVKSK TVVGHGRYRR SQVRAEMFGQ LTGGLEAAWS KLKGEEVLTK
110 120 130 140 150
DNIAEPMRDI RRALLEADVS LPVVRRFVQS VSDQAVGMGV IRGVKPDQQL
160 170 180 190 200
VKIVHDELVK LMGGEVSELQ FAKSGPTVIL LAGLQGVGKT TVCAKLACYL
210 220 230 240 250
KKQGKSCMLI AGDVYRPAAI DQLVILGEQV GVPVYTAGTD VKPADIAKQG
260 270 280 290 300
LKEAKKNNVD VVIMDTAGRL QIDKGMMDEL KDVKKFLNPT EVLLVVDAMT
310 320 330 340 350
GQEAAALVTT FNVEIGITGA ILTKLDGDSR GGAALSVKEV SGKPIKLVGR
360 370 380 390 400
GERMEDLEPF YPDRMAGRIL GMGDVLSFVE KATEVMRQED AEDLQKKIMS
410 420 430 440 450
AKFDFNDFLK QTRAVAKMGS MTRVLGMIPG MGKVSPAQIR EAEKNLLVME
460 470 480 490 500
AMIEVMTPEE RERPELLAES PERRKRIAKD SGKTEQQVSA LVAQIFQMRV
510 520 530 540 550
KMKNLMGVME GGSIPALSGL EDALKAEQKA PPGTARRKRK ADSRKKFVES
560
ASSKPGPRGF GSGN
Length:564
Mass (Da):61,232
Last modified:October 1, 1994 - v1
Checksum:i423F7285FB9063E4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761E → V in AAC64139 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS36637.
RefSeqiNP_196014.1. NM_120476.4.
UniGeneiAt.435.

Genome annotation databases

EnsemblPlantsiAT5G03940.1; AT5G03940.1; AT5G03940.
GeneIDi830273.
GrameneiAT5G03940.1; AT5G03940.1; AT5G03940.
KEGGiath:AT5G03940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS36637.
RefSeqiNP_196014.1. NM_120476.4.
UniGeneiAt.435.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HUGNMR-B530-543[»]
3UI2X-ray3.18B528-540[»]
ProteinModelPortaliP37107.
SMRiP37107. Positions 78-505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi15553. 4 interactions.
DIPiDIP-752N.
IntActiP37107. 4 interactions.
MINTiMINT-126488.
STRINGi3702.AT5G03940.1.

Protein family/group databases

TCDBi3.A.5.1.2. the general secretory pathway (sec) family.

Proteomic databases

PaxDbiP37107.
PRIDEiP37107.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G03940.1; AT5G03940.1; AT5G03940.
GeneIDi830273.
GrameneiAT5G03940.1; AT5G03940.1; AT5G03940.
KEGGiath:AT5G03940.

Organism-specific databases

TAIRiAT5G03940.

Phylogenomic databases

eggNOGiKOG0780. Eukaryota.
COG0541. LUCA.
HOGENOMiHOG000036164.
InParanoidiP37107.
KOiK03106.
OMAiMQKLMGM.
PhylomeDBiP37107.

Miscellaneous databases

EvolutionaryTraceiP37107.
PROiP37107.

Gene expression databases

GenevisibleiP37107. AT.

Family and domain databases

Gene3Di1.10.260.30. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00306. SRP54.
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]
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...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 530-543.

Entry informationi

Entry nameiSR54C_ARATH
AccessioniPrimary (citable) accession number: P37107
Secondary accession number(s): O82570
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: February 17, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.