EFG_LEGPH
ID EFG_LEGPH Reviewed; 694 AA.
AC Q5ZYP6;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Elongation factor G {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-G {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=lpg0326;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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; AE017354; AAU26423.1; -; Genomic_DNA.
DR RefSeq; WP_010946076.1; NC_002942.5.
DR RefSeq; YP_094370.1; NC_002942.5.
DR PDB; 5TY0; X-ray; 2.22 A; A=1-419.
DR PDBsum; 5TY0; -.
DR AlphaFoldDB; Q5ZYP6; -.
DR SMR; Q5ZYP6; -.
DR STRING; 272624.lpg0326; -.
DR PaxDb; Q5ZYP6; -.
DR PRIDE; Q5ZYP6; -.
DR EnsemblBacteria; AAU26423; AAU26423; lpg0326.
DR GeneID; 66489525; -.
DR KEGG; lpn:lpg0326; -.
DR PATRIC; fig|272624.6.peg.333; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_6; -.
DR OMA; AATTCHW; -.
DR Proteomes; UP000000609; 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..694
FT /note="Elongation factor G"
FT /id="PRO_0000091141"
FT DOMAIN 6..288
FT /note="tr-type G"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 86..90
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 140..143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:5TY0"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:5TY0"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:5TY0"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:5TY0"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:5TY0"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:5TY0"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:5TY0"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:5TY0"
FT TURN 193..197
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:5TY0"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:5TY0"
FT HELIX 210..224
FT /evidence="ECO:0007829|PDB:5TY0"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:5TY0"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:5TY0"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:5TY0"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:5TY0"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:5TY0"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 314..323
FT /evidence="ECO:0007829|PDB:5TY0"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 327..340
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:5TY0"
FT TURN 348..351
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:5TY0"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:5TY0"
SQ SEQUENCE 694 AA; 77026 MW; 8BB9E149E1D73783 CRC64;
MATPLKLYRN IGIAAHVDAG KTTTTERVLY YTGMSHKIGE VHDGAATMDW MVQEQERGIT
ITSAATTCYW SGMDKQFESH RINIIDTPGH VDFMIEVERS LRVLDGAVVV FDSVAGVEPQ
SETVWRQANK YGVPRIVFVN KMDRMGANFL RVVSQIKQRL GSTPVVLQLP IGAEEEFKGV
IDLIKMKAIH WDEENKGMTF KYVDIPADLK STCEEYRAHI IEAAAEYSEE LMEKYLEGEE
FTEAEIKKAL RHLTITNKVV PVFCGSAFKN KGVQAVLDGV IEYLPSPTDI PDIQGVDEHG
DVIHRKTSYD EPFSALAFKI ATDPFVGTLT YFRAYSGILK SGDTVYNSVK GKKERIGRLL
QMHANSREEI KEVRAGDIAA AVGLKTVTTG DTLCDQDKVV ILERMDFPDP VIAVAVEPKT
KADQEKMGIA LGKLAQEDPS FRVHTDEESG QTIIQGMGEL HLEIIVDRMK REFNVEANVG
KPQVAYRETL KQAVEQEGKF VRQSGGRGQY GHVWLKIEPQ EPGKGYEFIN AIVGGVIPKE
YIPAVDKGIQ EQMQNGVIAG YPVVDVKVTL FDGSFHEVDS SEMAFKIAGS QCFKQGALKA
KPVLLEPIMS VEVVTPEDYM GDVMGDLNRR RGLVQGMEDS PAGKIVRAEV PLAEMFGYST
DLRSATQGRA TYTMEFCKYA EAPTNIAEAI IKKQ
