EFGC_ARATH
ID EFGC_ARATH Reviewed; 783 AA.
AC Q9SI75; Q94BR7;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Elongation factor G, chloroplastic {ECO:0000255|HAMAP-Rule:MF_03063};
DE Short=cEF-G {ECO:0000255|HAMAP-Rule:MF_03063};
DE AltName: Full=Elongation factor EF-G/SCO1;
DE AltName: Full=Protein SNOWY COTYLEDON 1, chloroplastic;
DE Short=AtSCO1;
DE Flags: Precursor;
GN Name=CPEFG; Synonyms=SCO1; OrderedLocusNames=At1g62750; ORFNames=F23N19.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF GLY-132, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=16525888; DOI=10.1007/s11103-005-4921-0;
RA Albrecht V., Ingenfeld A., Apel K.;
RT "Characterization of the snowy cotyledon 1 mutant of Arabidopsis thaliana:
RT the impact of chloroplast elongation factor G on chloroplast development
RT and plant vitality.";
RL Plant Mol. Biol. 60:507-518(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-132, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17629920; DOI=10.1186/1471-2229-7-37;
RA Ruppel N.J., Hangarter R.P.;
RT "Mutations in a plastid-localized elongation factor G alter early stages of
RT plastid development in Arabidopsis thaliana.";
RL BMC Plant Biol. 7:37-37(2007).
CC -!- FUNCTION: Chloroplast-localized elongation factor EF-G involved in
CC protein synthesis in plastids. Catalyzes the GTP-dependent ribosomal
CC translocation step during translation elongation. During this step, the
CC ribosome changes from the pre-translocational (PRE) to the post-
CC translocational (POST) state as the newly formed A-site-bound peptidyl-
CC tRNA and P-site-bound deacylated tRNA move to the P and E sites,
CC respectively. Catalyzes the coordinated movement of the two tRNA
CC molecules, the mRNA and conformational changes in the ribosome.
CC Required for the eoplasts redifferentiation into chloroplasts after
CC germination. {ECO:0000255|HAMAP-Rule:MF_03063,
CC ECO:0000269|PubMed:16525888, ECO:0000269|PubMed:17629920}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000255|HAMAP-Rule:MF_03063}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_03063, ECO:0000269|PubMed:16525888,
CC ECO:0000269|PubMed:17629920}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons and at lower levels in
CC adult leaves. {ECO:0000269|PubMed:17629920}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality. {ECO:0000269|PubMed:17629920}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03063}.
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DR EMBL; BK005771; DAA05753.1; -; mRNA.
DR EMBL; AC007190; AAF19548.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34000.1; -; Genomic_DNA.
DR EMBL; AY142646; AAN13104.1; -; mRNA.
DR EMBL; AY039936; AAK64040.1; -; mRNA.
DR PIR; E96652; E96652.
DR RefSeq; NP_564801.1; NM_104952.2.
DR AlphaFoldDB; Q9SI75; -.
DR SMR; Q9SI75; -.
DR BioGRID; 27794; 1.
DR STRING; 3702.AT1G62750.1; -.
DR MetOSite; Q9SI75; -.
DR PaxDb; Q9SI75; -.
DR PRIDE; Q9SI75; -.
DR ProteomicsDB; 221963; -.
DR EnsemblPlants; AT1G62750.1; AT1G62750.1; AT1G62750.
DR GeneID; 842573; -.
DR Gramene; AT1G62750.1; AT1G62750.1; AT1G62750.
DR KEGG; ath:AT1G62750; -.
DR Araport; AT1G62750; -.
DR TAIR; locus:2026212; AT1G62750.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; Q9SI75; -.
DR OMA; MDDMVGG; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; Q9SI75; -.
DR UniPathway; UPA00345; -.
DR PRO; PR:Q9SI75; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SI75; baseline and differential.
DR Genevisible; Q9SI75; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR GO; GO:0009791; P:post-embryonic development; IMP:TAIR.
DR GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR HAMAP; MF_03063; EF_G_plantC; 1.
DR InterPro; IPR030848; EF_G_plantC.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR035649; EFG_V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004540; Transl_elong_EFG/EF2.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00484; EF-G; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Elongation factor; GTP-binding; Nucleotide-binding; Plastid;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..80
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
FT CHAIN 81..783
FT /note="Elongation factor G, chloroplastic"
FT /id="PRO_0000423632"
FT DOMAIN 94..369
FT /note="tr-type G"
FT BINDING 103..110
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
FT BINDING 167..171
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
FT BINDING 221..224
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03063"
FT MUTAGEN 132
FT /note="G->R: In sco1-1; chlorotic cotyledons and green true
FT leaves, and delayed development and germination."
FT /evidence="ECO:0000269|PubMed:16525888,
FT ECO:0000269|PubMed:17629920"
FT CONFLICT 186
FT /note="D -> G (in Ref. 4; AAK64040)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 783 AA; 86058 MW; 3117557E49DC0746 CRC64;
MAADALRISS SSSGSLVCNL NGSQRRPVLL PLSHRATFLG LPPRASSSSI SSSIPQFLGT
SRIGLGSSKL SQKKKQFSVF AAAEAEAKRA VPLKDYRNIG IMAHIDAGKT TTTERILYYT
GRNYKIGEVH EGTATMDWME QEQERGITIT SAATTTFWDK HRINIIDTPG HVDFTLEVER
ALRVLDGAIC LFDSVAGVEP QSETVWRQAD KYGVPRICFV NKMDRLGANF FRTRDMIVTN
LGAKPLVLQI PIGAEDVFKG VVDLVRMKAI VWSGEELGAK FSYEDIPEDL EDLAQEYRAA
MMELIVDLDD EVMENYLEGV EPDEATVKRL VRKGTITGKF VPILCGSAFK NKGVQPLLDA
VVDYLPSPVE VPPMNGTDPE NPEITIIRKP DDDEPFAGLA FKIMSDPFVG SLTFVRVYSG
KISAGSYVLN ANKGKKERIG RLLEMHANSR EDVKVALTGD IIALAGLKDT ITGETLSDPE
NPVVLERMDF PDPVIKVAIE PKTKADIDKM ATGLIKLAQE DPSFHFSRDE EMNQTVIEGM
GELHLEIIVD RLKREFKVEA NVGAPQVNYR ESISKIAEVK YTHKKQSGGQ GQFADITVRF
EPLEAGSGYE FKSEIKGGAV PREYIPGVMK GLEECMSTGV LAGFPVVDVR ACLVDGSYHD
VDSSVLAFQL AARGAFREGM RKAGPRMLEP IMRVEVVTPE EHLGDVIGDL NSRRGQINSF
GDKPGGLKVV DSLVPLAEMF QYVSTLRGMT KGRASYTMQL AKFDVVPQHI QNQLSSKDQE
VAA
