EFG1_PSEAE
ID EFG1_PSEAE Reviewed; 706 AA.
AC Q9HWD2;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Elongation factor G 1 {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-G 1 {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; Synonyms=fusA1;
GN OrderedLocusNames=PA4266;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG07654.1; -; Genomic_DNA.
DR PIR; D83112; D83112.
DR RefSeq; NP_252956.1; NC_002516.2.
DR RefSeq; WP_003093741.1; NZ_QZGE01000028.1.
DR PDB; 4FN5; X-ray; 2.90 A; A=1-706.
DR PDBsum; 4FN5; -.
DR AlphaFoldDB; Q9HWD2; -.
DR SMR; Q9HWD2; -.
DR STRING; 287.DR97_3645; -.
DR PaxDb; Q9HWD2; -.
DR PRIDE; Q9HWD2; -.
DR DNASU; 881744; -.
DR EnsemblBacteria; AAG07654; AAG07654; PA4266.
DR GeneID; 881744; -.
DR KEGG; pae:PA4266; -.
DR PATRIC; fig|208964.12.peg.4467; -.
DR PseudoCAP; PA4266; -.
DR HOGENOM; CLU_002794_4_1_6; -.
DR InParanoid; Q9HWD2; -.
DR OMA; AATTCHW; -.
DR PhylomeDB; Q9HWD2; -.
DR BioCyc; PAER208964:G1FZ6-4339-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
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..706
FT /note="Elongation factor G 1"
FT /id="PRO_0000091184"
FT DOMAIN 8..290
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 88..92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 142..145
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:4FN5"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 23..39
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:4FN5"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 166..176
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:4FN5"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 209..227
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:4FN5"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:4FN5"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:4FN5"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:4FN5"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 428..441
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 446..450
FT /evidence="ECO:0007829|PDB:4FN5"
FT TURN 451..454
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 455..461
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 463..474
FT /evidence="ECO:0007829|PDB:4FN5"
FT TURN 475..477
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 498..509
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 512..523
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 536..541
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 553..566
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 568..571
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 574..583
FT /evidence="ECO:0007829|PDB:4FN5"
FT TURN 588..590
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 593..605
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 607..610
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 614..627
FT /evidence="ECO:0007829|PDB:4FN5"
FT TURN 628..630
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 631..638
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 639..641
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 644..650
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 652..663
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 664..666
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 669..676
FT /evidence="ECO:0007829|PDB:4FN5"
FT TURN 677..679
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:4FN5"
FT STRAND 687..692
FT /evidence="ECO:0007829|PDB:4FN5"
FT HELIX 695..703
FT /evidence="ECO:0007829|PDB:4FN5"
SQ SEQUENCE 706 AA; 77784 MW; 6A56DA5F41582283 CRC64;
MARTTPINRY RNIGICAHVD AGKTTTTERV LFYTGVNHKL GEVHDGAATT DWMVQEQERG
ITITSAAVTT FWKGSRGQYD NYRVNVIDTP GHVDFTIEVE RSLRVLDGAV VVFCGTSGVE
PQSETVWRQA NKYGVPRIVY VNKMDRQGAN FLRVVEQIKK RLGHTPVPVQ LAIGAEENFV
GQVDLIKMKA IYWNDDDKGM TYREEEIPAE LKDLAEEWRS SMVEAAAEAN EELMNKYLEE
GELSEAEIKE GLRLRTLACE IVPAVCGSSF KNKGVPLVLD AVIDYLPAPT EIPAIKGVSP
DDETVEDERH ADDNEPFSSL AFKIATDPFV GTLTFARVYS GVLSSGDSVL NSVKGKKERV
GRMVQMHANQ REEIKEVRAG DIAALIGMKD VTTGDTLCSI EKPIILERMD FPEPVISVAV
EPKTKADQEK MGIALGKLAQ EDPSFRVKTD EESGQTIISG MGELHLDIIV DRMKREFGVE
ANIGKPQVAY RETITKDNVE IEGKFVRQSG GRGQFGHCWI RFSAADVDEK GNITEGLVFE
NEVVGGVVPK EYIPAIQKGI EEQMKNGVVA GYPLIGLKAT VFDGSYHDVD SNEMAFKIAA
SMATKQLAQK GGGKVLEPIM KVEVVTPEDY MGDVMGDLNR RRGLIQGMED TVSGKVIRAE
VPLGEMFGYA TDVRSMSQGR ASYSMEFSKY AEAPSNIVEA LVKKQG
