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Protein

Cell division protein FtsY homolog, chloroplastic

Gene

CPFTSY

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

Functioni

Signal recognition particle receptor protein. Binds GTP specifically. The GTPase activity is inhibited by the N-terminus of the protein until binding to the thylakoid membrane. Activates the GTPase activity of FFC/cpSRP54 when bound to the cpSRP complex. Required for light-harvesting chlorophyll a/b-binding protein (LHCP) integration into thylakoids. Might be also functionally linked to the Sec translocation machinery.6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi171 – 1788GTPBy similarity
Nucleotide bindingi254 – 2585GTPBy similarity
Nucleotide bindingi318 – 3214GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

GTP-binding, Metal-binding, Nucleotide-binding

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division protein FtsY homolog, chloroplastic
Alternative name(s):
Chloroplast SRP receptor homolog, alpha subunit CpFtsY
Fused signal recognition particle receptor
Gene namesi
Name:CPFTSY
Synonyms:FTSY
Ordered Locus Names:At2g45770
ORF Names:F4I18.25
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G45770.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Thylakoid

Pathology & Biotechi

Disruption phenotypei

Seedling lethal.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi48 – 481F → A: Reduced binding to the thylakoid and 80% reduction of LHCP integration in thylakoids, but no effect on GTP binding. Reduced binding to the thylakoid and 80% reduction of LHCP integration in thylakoids; when associated with A-49.
Mutagenesisi48 – 481F → G, E, Q or K: Severe reduction of LHCP integration in thylakoids.
Mutagenesisi48 – 481F → L, V, Y or W: No or limited reduction of LHCP integration in thylakoids.
Mutagenesisi49 – 491F → A: Reduced binding to the thylakoid and 40% reduction of LHCP integration in thylakoids. Reduced binding to the thylakoid and 80% reduction of LHCP integration in thylakoids; when associated with A-48.
Mutagenesisi51 – 511R → A: Reduced binding to the thylakoid and LHCP integration in thylakoids; when associated with A-54. 1 Publication
Mutagenesisi52 – 521L → A or Q: Reduced binding to the thylakoid and LHCP integration in thylakoids. 1 Publication
Mutagenesisi54 – 541R → A: Reduced binding to the thylakoid and LHCP integration in thylakoids; when associated with A-51. 1 Publication
Mutagenesisi56 – 561I → A: Reduced binding to the thylakoid and LHCP integration in thylakoids. 1 Publication
Mutagenesisi71 – 711F → V, A or L: Reduced interaction with FFC, but no effect on the basal GTPase activity. 2 Publications
Mutagenesisi109 – 1091F → V: Reduced interaction with FFC. 1 Publication
Mutagenesisi321 – 3211D → N: Loss of GTP binding specificity. 1 Publication
Mutagenesisi326 – 3261G → W: Reduced interaction with FFC, but no effect on the basal GTPase activity. 1 Publication
Mutagenesisi344 – 3441G → D in frd4-2; chlorotic and reduction in thylakoid membrane content and stacking. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040ChloroplastSequence analysisAdd
BLAST
Chaini41 – 366326Cell division protein FtsY homolog, chloroplasticPRO_0000413416Add
BLAST

Proteomic databases

PaxDbiO80842.
PRIDEiO80842.

PTM databases

iPTMnetiO80842.

Expressioni

Tissue specificityi

Expressed in green tissues. Low levels in roots and seeds.2 Publications

Developmental stagei

Peak of expression 20 days after germination.1 Publication

Inductioni

Not induced by light or iron.2 Publications

Interactioni

Subunit structurei

Monomer. Interacts with FFC/cpSRP54, a component of the cpSRP complex, composed of a FFC/cpSRP54 monomer and a CAO/cpSRP43 dimer. The complex with FFC/cpSRP54 is formed when both proteins are bound with GTP.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ALB3Q8LBP42EBI-2353373,EBI-1806831

Protein-protein interaction databases

BioGridi4521. 5 interactions.
IntActiO80842. 6 interactions.
MINTiMINT-7993024.
STRINGi3702.AT2G45770.2.

Structurei

Secondary structure

1
366
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi66 – 705Combined sources
Helixi72 – 787Combined sources
Helixi80 – 856Combined sources
Helixi90 – 923Combined sources
Helixi93 – 10614Combined sources
Helixi111 – 12616Combined sources
Helixi133 – 14816Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi165 – 1706Combined sources
Helixi177 – 19014Combined sources
Beta strandi195 – 1984Combined sources
Helixi205 – 21814Combined sources
Beta strandi221 – 2233Combined sources
Beta strandi226 – 2294Combined sources
Helixi232 – 24514Combined sources
Beta strandi249 – 2535Combined sources
Helixi263 – 27715Combined sources
Beta strandi285 – 2928Combined sources
Helixi293 – 2997Combined sources
Helixi300 – 30910Combined sources
Beta strandi314 – 3185Combined sources
Helixi327 – 33610Combined sources
Beta strandi340 – 3445Combined sources
Beta strandi346 – 3483Combined sources
Helixi349 – 3513Combined sources
Beta strandi352 – 3543Combined sources
Helixi357 – 3659Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OG2X-ray2.00A41-366[»]
3B9QX-ray1.75A65-366[»]
ProteinModelPortaliO80842.
SMRiO80842. Positions 65-366.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO80842.

Family & Domainsi

Domaini

The N-terminal domain (39-56) is necessary and sufficient for thylakoid binding.1 Publication

Sequence similaritiesi

Belongs to the GTP-binding SRP family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IQAY. Eukaryota.
COG0552. LUCA.
HOGENOMiHOG000036278.
InParanoidiO80842.
KOiK03110.
PhylomeDBiO80842.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR013822. Signal_recog_particl_SRP54_hlx.
IPR004390. SR_rcpt_FtsY.
IPR000897. SRP54_GTPase_dom.
[Graphical view]
PfamiPF00448. SRP54. 1 hit.
PF02881. SRP54_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00962. SRP54. 1 hit.
SM00963. SRP54_N. 1 hit.
[Graphical view]
SUPFAMiSSF47364. SSF47364. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00064. ftsY. 1 hit.
PROSITEiPS00300. SRP54. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: O80842-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATSSAHLSF LAGRISPFSS ERIGLFPLRG EFRPRMTRFR CSAGPSGFFT
60 70 80 90 100
RLGRLIKEKA KSDVEKVFSG FSKTRENLAV IDELLLFWNL AETDRVLDEL
110 120 130 140 150
EEALLVSDFG PKITVRIVER LREDIMSGKL KSGSEIKDAL KESVLEMLAK
160 170 180 190 200
KNSKTELQLG FRKPAVIMIV GVNGGGKTTS LGKLAHRLKN EGTKVLMAAG
210 220 230 240 250
DTFRAAASDQ LEIWAERTGC EIVVAEGDKA KAATVLSKAV KRGKEEGYDV
260 270 280 290 300
VLCDTSGRLH TNYSLMEELI ACKKAVGKIV SGAPNEILLV LDGNTGLNML
310 320 330 340 350
PQAREFNEVV GITGLILTKL DGSARGGCVV SVVEELGIPV KFIGVGEAVE
360
DLQPFDPEAF VNAIFS
Length:366
Mass (Da):39,679
Last modified:June 1, 2002 - v2
Checksum:i8986F431A6A3BE12
GO

Sequence cautioni

The sequence AEC10600.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81L → F (Ref. 2) Curated
Sequence conflicti8 – 81L → F in AAD47910 (PubMed:18022392).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010820 mRNA. Translation: CAB40382.1.
AF120112 mRNA. Translation: AAD47910.1.
AC004665 Genomic DNA. Translation: AAC28547.2.
CP002685 Genomic DNA. Translation: AEC10599.1.
CP002685 Genomic DNA. Translation: AEC10600.1. Sequence problems.
AF360125 mRNA. Translation: AAK25835.1.
AY051026 mRNA. Translation: AAK93703.1.
PIRiT02470.
T52612.
RefSeqiNP_001189754.1. NM_001202825.1.
NP_566056.1. NM_130140.2. [O80842-1]
UniGeneiAt.491.

Genome annotation databases

EnsemblPlantsiAT2G45770.1; AT2G45770.1; AT2G45770. [O80842-1]
GeneIDi819185.
KEGGiath:AT2G45770.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010820 mRNA. Translation: CAB40382.1.
AF120112 mRNA. Translation: AAD47910.1.
AC004665 Genomic DNA. Translation: AAC28547.2.
CP002685 Genomic DNA. Translation: AEC10599.1.
CP002685 Genomic DNA. Translation: AEC10600.1. Sequence problems.
AF360125 mRNA. Translation: AAK25835.1.
AY051026 mRNA. Translation: AAK93703.1.
PIRiT02470.
T52612.
RefSeqiNP_001189754.1. NM_001202825.1.
NP_566056.1. NM_130140.2. [O80842-1]
UniGeneiAt.491.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OG2X-ray2.00A41-366[»]
3B9QX-ray1.75A65-366[»]
ProteinModelPortaliO80842.
SMRiO80842. Positions 65-366.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4521. 5 interactions.
IntActiO80842. 6 interactions.
MINTiMINT-7993024.
STRINGi3702.AT2G45770.2.

Protein family/group databases

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

PTM databases

iPTMnetiO80842.

Proteomic databases

PaxDbiO80842.
PRIDEiO80842.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G45770.1; AT2G45770.1; AT2G45770. [O80842-1]
GeneIDi819185.
KEGGiath:AT2G45770.

Organism-specific databases

TAIRiAT2G45770.

Phylogenomic databases

eggNOGiENOG410IQAY. Eukaryota.
COG0552. LUCA.
HOGENOMiHOG000036278.
InParanoidiO80842.
KOiK03110.
PhylomeDBiO80842.

Miscellaneous databases

EvolutionaryTraceiO80842.
PROiO80842.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR013822. Signal_recog_particl_SRP54_hlx.
IPR004390. SR_rcpt_FtsY.
IPR000897. SRP54_GTPase_dom.
[Graphical view]
PfamiPF00448. SRP54. 1 hit.
PF02881. SRP54_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00962. SRP54. 1 hit.
SM00963. SRP54_N. 1 hit.
[Graphical view]
SUPFAMiSSF47364. SSF47364. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00064. ftsY. 1 hit.
PROSITEiPS00300. SRP54. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Involvement of a chloroplast homologue of the signal recognition particle receptor protein, FtsY, in protein targeting to thylakoids."
    Kogata N., Nishio K., Hirohashi T., Kikuchi S., Nakai M.
    FEBS Lett. 447:329-333(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
  2. "CPFTSY signal recognition particle receptor homolog."
    Peterson E.C., Henry R.L.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Wassilewskija.
  3. 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. "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, SUBCELLULAR LOCATION, SUBUNIT.
  7. "ATP stimulates signal recognition particle (SRP)/FtsY-supported protein integration in chloroplasts."
    Yuan J., Kight A., Goforth R.L., Moore M., Peterson E.C., Sakon J., Henry R.
    J. Biol. Chem. 277:32400-32404(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Functional interaction of chloroplast SRP/FtsY with the ALB3 translocase in thylakoids: substrate not required."
    Moore M., Goforth R.L., Mori H., Henry R.
    J. Cell Biol. 162:1245-1254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ALB3.
  9. "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: MUTAGENESIS OF GLY-344, TISSUE SPECIFICITY, INDUCTION BY IRON, SUBCELLULAR LOCATION.
  10. "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, MUTAGENESIS OF ASP-321, INTERACTION WITH CPSRP54/FFC.
  11. "Non-identical contributions of two membrane-bound cpSRP components, cpFtsY and Alb3, to thylakoid biogenesis."
    Asakura Y., Kikuchi S., Nakai M.
    Plant J. 56:1007-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, INDUCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  12. "The membrane-binding motif of the chloroplast signal recognition particle receptor (cpFtsY) regulates GTPase activity."
    Marty N.J., Rajalingam D., Kight A.D., Lewis N.E., Fologea D., Kumar T.K., Henry R.L., Goforth R.L.
    J. Biol. Chem. 284:14891-14903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, MUTAGENESIS OF 48-PHE-PHE-49; ARG-51; LEU-52; ARG-54 AND ILE-56, STRUCTURE BY NMR OF 39-56.
  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 CPSRP54/FFC, MUTAGENESIS OF PHE-71 AND GLY-326.
  14. "Molecular dynamics simulation reveals preorganization of the chloroplast FtsY towards complex formation induced by GTP binding."
    Yang M.J., Pang X.Q., Zhang X., Han K.L.
    J. Struct. Biol. 173:57-66(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  15. "The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting site."
    Stengel K.F., Holdermann I., Wild K., Sinning I.
    FEBS Lett. 581:5671-5676(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 65-366.
  16. "Structure of the chloroplast signal recognition particle (cpSRP) receptor: domain arrangement modulates SRP-receptor interaction."
    Chandrasekar S., Chartron J., Jaru-Ampornpan P., Shan S.O.
    J. Mol. Biol. 375:425-436(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 41-366, MUTAGENESIS OF PHE-71 AND PHE-109.

Entry informationi

Entry nameiCFTSY_ARATH
AccessioniPrimary (citable) accession number: O80842
Secondary accession number(s): F4IH43, Q9SWS7, Q9XFR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: June 1, 2002
Last modified: February 17, 2016
This is version 120 of the entry and version 2 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.