ID   EFG_LISMC               Reviewed;         695 AA.
AC   C1KZK7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Lm4b_02626;
OS   Listeria monocytogenes serotype 4b (strain CLIP80459).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=568819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIP80459;
RX   PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA   Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA   Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A.,
RA   Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P.,
RA   Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT   "Comparative genomics and transcriptomics of lineages I, II, and III
RT   strains of Listeria monocytogenes.";
RL   BMC Genomics 13:144-144(2012).
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; FM242711; CAS06380.1; -; Genomic_DNA.
DR   RefSeq; WP_003724965.1; NC_012488.1.
DR   AlphaFoldDB; C1KZK7; -.
DR   SMR; C1KZK7; -.
DR   GeneID; 67411090; -.
DR   KEGG; lmc:Lm4b_02626; -.
DR   HOGENOM; CLU_002794_4_1_9; -.
DR   OMA; AATTCHW; -.
DR   BioCyc; LMON568819:LM4B_RS13395-MON; -.
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   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..695
FT                   /note="Elongation factor G"
FT                   /id="PRO_1000202305"
FT   DOMAIN          8..282
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         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         135..138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   695 AA;  76850 MW;  FD9D79E53C023C30 CRC64;
     MAREFSLEKT RNIGIMAHID AGKTTTTERI LFYTGRIHKI GETHEGASQM DWMEQEQERG
     ITITSAATTA QWKGYRVNII DTPGHVDFTV EVERSLRVLD GAVAVLDAQS GVEPQTETVW
     RQATTYGVPR VVFVNKMDKI GADFLYSVGT LHERLAANAH PIQLPIGAED TFEGIIDLIE
     MNALYYEDDL GNDPHIKEIP ADLKDLADEY RGKLVEAVAE LDEELMMKYL EGEEITKEEL
     KAGIRKGTLN VEFYPVVCGT AFKNKGVQPM LDAVLDYLPA PTDVPAINGV LPDGEEAARH
     ADDSEPFSSL AFKVMTDPYV GRLTFFRVYS GTLNSGSYVQ NSTKGKRERV GRILQMHANH
     REEISIVYAG DIAAAVGLKD TTTGDTLCDE KEQIILESME FPEPVIQVAI EPKSKADQDK
     MGQALAKLAE EDPTFRAETD QETGQTLISG MGELHLDILV DRMRREFRVE ANVGDPQVSY
     RETFRKSAQV EGKFVRQSGG RGQYGHVWIE FGPNEEGKGF EFENAIVGGV VPREYIPAVQ
     AGLEGALDNG VLAGYPLIDI KAKLYDGSYH DVDSNEMAFK VAASMALRNA AKKCDPVILE
     PMMAVEVVIP EEYLGDIMGN ITSRRGRVDG MEARGNAQVV RAFVPLANMF GYATHLRSGT
     QGRGVYTMQF DHYEEVPKSI AEEIIKANGG NNKED