ID EF2_DICDI Reviewed; 839 AA.
AC P15112; Q54J09;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 27-MAR-2024, entry version 163.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P32324};
GN Name=efbA; ORFNames=DDB_G0288373;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2475501; DOI=10.1016/s0021-9258(19)84856-1;
RA Toda K., Tasaka M., Mashima K., Kohno K., Uchida T., Takeuchi I.;
RT "Structure and expression of elongation factor 2 gene during development of
RT Dictyostelium discoideum.";
RL J. Biol. Chem. 264:15489-15493(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP PROTEIN SEQUENCE OF 2-10; 33-55; 285-293; 300-315; 464-477; 481-488;
RP 700-709; 760-768 AND 812-820, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Patel H., Brunton V.G., Frame M.C.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome. {ECO:0000250|UniProtKB:P32324}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:P32324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P32324};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32324}.
CC -!- PTM: Phosphorylation by EF-2 kinase completely inactivates EF-2.
CC {ECO:0000250|UniProtKB:P13639}.
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|PROSITE-ProRule:PRU01059}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA33205.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M26017; AAA33205.1; ALT_FRAME; mRNA.
DR EMBL; AAFI02000111; EAL63212.1; -; Genomic_DNA.
DR PIR; A34347; A34347.
DR RefSeq; XP_636721.1; XM_631629.1.
DR AlphaFoldDB; P15112; -.
DR SMR; P15112; -.
DR STRING; 44689.P15112; -.
DR PaxDb; 44689-DDB0191363; -.
DR EnsemblProtists; EAL63212; EAL63212; DDB_G0288373.
DR GeneID; 8626597; -.
DR KEGG; ddi:DDB_G0288373; -.
DR dictyBase; DDB_G0288373; efbA.
DR eggNOG; KOG0469; Eukaryota.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; P15112; -.
DR OMA; NRHNRFY; -.
DR PhylomeDB; P15112; -.
DR Reactome; R-DDI-156902; Peptide chain elongation.
DR Reactome; R-DDI-5358493; Synthesis of diphthamide-EEF2.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-8876725; Protein methylation.
DR PRO; PR:P15112; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd04096; eEF2_snRNP_like_C; 1.
DR CDD; cd01885; EF2; 1.
DR CDD; cd16268; EF2_II; 1.
DR CDD; cd16261; EF2_snRNP_III; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_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; IPR005517; Transl_elong_EFG/EF2_IV.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42908:SF10; ELONGATION FACTOR 2; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
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; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW Hydrolase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..839
FT /note="Elongation factor 2"
FT /id="PRO_0000091011"
FT DOMAIN 17..248
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 26..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32324"
FT BINDING 156..159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32324"
FT BINDING 211..213
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32324"
FT MOD_RES 698
FT /note="Diphthamide"
FT /evidence="ECO:0000250|UniProtKB:P32324"
FT CONFLICT 233
FT /note="V -> D (in Ref. 1; AAA33205)"
FT /evidence="ECO:0000305"
FT CONFLICT 566..586
FT /note="Missing (in Ref. 1; AAA33205)"
FT /evidence="ECO:0000305"
FT CONFLICT 777..778
FT /note="FG -> LR (in Ref. 1; AAA33205)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="D -> A (in Ref. 1; AAA33205)"
FT /evidence="ECO:0000305"
FT CONFLICT 837..839
FT /note="EKL -> RKTINNLSHTLSFQI (in Ref. 1; AAA33205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 839 AA; 92659 MW; 8F1F859D757533F1 CRC64;
MVNFTIDQIR AIMDRRENIR NMSVIAHVDH GKTTLSDSLI QRAGIIADKV SGDMRYMSCR
ADEQERGITI KSSSVSLHFE MPKEDKLPAG CTSHEFLINL IDSPGHVDFS SEVTAALRVT
DGALVVIDCV EGVCVQTETV LRQAVAERIK PVLFVNKVDR FLLELQLNTE EAYLSFRRAI
ESVNVIVGNT EDKEFGDVTV SPEKGTVAFG SGLHGWGFTL GRFAKLYAAK FGVPEDKLMG
RLWGDSYFDA TAKKWTSNPQ SADGKALPRA FCQFVLEPIY QLTRAIVDED AVKLEKMMKT
LQITLAPEDA EIKGKQLVKA VMRKFLPAAD AILSMIVTHL PSPLVAQKYR CANLYEGPMD
DECAVAIQKC DPNGPLMMYV SKMVPTSDKG RFYAFGRVFS GIIRTGQKVR IMGVNYVPGK
KDDLFLKSIQ RTVLMMGRKT EQIEDCPCGN IVGLVGVDQF LVKSGTITTS EVAHNIRVMK
FSVSPVVRVA VEPKNPSDLP KLVEGLKRLA KSDPCVLCYS EESGEHIVAG AGELHLEICL
KDLAEDHAGI EIKTTDPVVS FRESVSEESS IMCLSKSPNK HNRLFMKASP ISMELQDLIE
AGSDISSKDD PKARANYLAD NHEWDKNDAM NIWSFGPEGN GANLLVNVTK GVQYLNEIKD
SFVGAFQWAT KEGVVCDENM RGIRFNLYDV TLHTDAIHRG GGQIIPTARR VLYAAELTAS
PTLLEPIYLV EITAPENAIG GIYSVLNRRR GIVIGEERRI GSPLFSVKAH LPVLESFGFT
ADLRSHTAGQ AFPQCVFDHW ASIGVVNKDK KATEVALATR KRKGLAPEIP DLDKFHEKL
//
