EFG2_PSEPK
ID EFG2_PSEPK Reviewed; 703 AA.
AC Q88FI4;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Elongation factor G 2 {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-G 2 {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusB; Synonyms=fusA-2; OrderedLocusNames=PP_4111;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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:0000255|HAMAP-
CC Rule:MF_00054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00054}.
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_00054}.
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DR EMBL; AE015451; AAN69695.1; -; Genomic_DNA.
DR RefSeq; NP_746231.1; NC_002947.4.
DR RefSeq; WP_010954893.1; NC_002947.4.
DR PDB; 6N0I; X-ray; 2.60 A; A/B=1-703.
DR PDBsum; 6N0I; -.
DR AlphaFoldDB; Q88FI4; -.
DR SMR; Q88FI4; -.
DR STRING; 160488.PP_4111; -.
DR PRIDE; Q88FI4; -.
DR EnsemblBacteria; AAN69695; AAN69695; PP_4111.
DR KEGG; ppu:PP_4111; -.
DR PATRIC; fig|160488.4.peg.4369; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_6; -.
DR OMA; NHKMGEV; -.
DR PhylomeDB; Q88FI4; -.
DR BioCyc; PPUT160488:G1G01-4378-MON; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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 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 3D-structure; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..703
FT /note="Elongation factor G 2"
FT /id="PRO_0000091187"
FT DOMAIN 8..291
FT /note="tr-type G"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 89..93
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 143..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 10..17
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:6N0I"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 122..133
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:6N0I"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 210..228
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:6N0I"
FT TURN 270..273
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:6N0I"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 319..328
FT /evidence="ECO:0007829|PDB:6N0I"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 332..345
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:6N0I"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 372..379
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 417..425
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 426..442
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 447..450
FT /evidence="ECO:0007829|PDB:6N0I"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 457..463
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 464..476
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 499..507
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 514..523
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 531..538
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 548..561
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 563..566
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 569..579
FT /evidence="ECO:0007829|PDB:6N0I"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 588..600
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 602..605
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 609..621
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 626..635
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 649..657
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 658..660
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 664..672
FT /evidence="ECO:0007829|PDB:6N0I"
FT STRAND 677..687
FT /evidence="ECO:0007829|PDB:6N0I"
FT HELIX 690..697
FT /evidence="ECO:0007829|PDB:6N0I"
SQ SEQUENCE 703 AA; 77833 MW; 0DB372A9867DE1BE CRC64;
MARTTPIELY RNIGIVAHVD AGKTTTTERI LFYTGVNHKM GEVHDGAATM DWMAQEQERG
ITITSAATTA FWQGSTKQFA HKYRFNIIDT PGHVDFTIEV ERSLRVLDGA VVVFSGADGV
EPQSETVWRQ ANKYHVPRLA YINKMDRQGA DFLRVVKQID QRLGHHPVPI QLAIGSEENF
MGQIDLVKMK AIYWNDADQG TSYREEEIPA ELKALADEWR AHMIEAAAEA NDELTMKFLD
GEELSIEEIK AGLRQRTIAN EIVPTILGSS FKNKGVPLML DAVIDYLPAP SEIPAIRGTD
PDDEEKHLER HADDKEPFSA LAFKIATDPF VGTLTFARVY SGVLSSGNAV LNSVKGKKER
IGRMVQMHAN QRAEIKDVCA GDIAALIGMK DVTTGDTLCD MDKPIILERM DFPDPVISVA
VEPKTKADQE KMGIALGKLA QEDPSFRVRT DEETGQTIIS GMGELHLDII VDRMRREFNV
EANIGKPQVA YREKIRNTCE IEGRFVRQSG GRGQYGHCWI RFAPGDEGKE GLEFINEIVG
GVVPREYIPA IQKGIEEQMK NGVLAGYPLI NLKAAVFDGS YHDVDSNEMA YKIAASMATK
QLSQKGGAVL LEPVMKVEVV TPEEYQGDIL GDLSRRRGMI QDGDETPAGK VIRAEVPLGE
MFGYATSMRS MTQGRASFSM EFTRYAEAPA SIADGIVKKS RGE
