EFG_LACLM
ID EFG_LACLM Reviewed; 709 AA.
AC A2RP72;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=llmg_2556;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
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; AM406671; CAL99118.1; -; Genomic_DNA.
DR RefSeq; WP_011836173.1; NZ_WJVF01000037.1.
DR AlphaFoldDB; A2RP72; -.
DR SMR; A2RP72; -.
DR STRING; 416870.llmg_2556; -.
DR PRIDE; A2RP72; -.
DR EnsemblBacteria; CAL99118; CAL99118; llmg_2556.
DR GeneID; 61110607; -.
DR KEGG; llm:llmg_2556; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_9; -.
DR OMA; AATTCHW; -.
DR PhylomeDB; A2RP72; -.
DR BioCyc; LLAC416870:LLMG_RS12890-MON; -.
DR Proteomes; UP000000364; 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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..709
FT /note="Elongation factor G"
FT /id="PRO_1000008839"
FT DOMAIN 8..297
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 709 AA; 77972 MW; 8EAD29D37E6B7FCD CRC64;
MAREFSLANT RNIGIMAHVD AGKTTTTERV LYYTGKIHKI GETHEGASQM DWMEQEQERG
ITITSAATTA EWKGNRVNII DTPGHVDFTI EVQRSLRVLD GAVTVLDAQS GVEPQTETVW
RQATEYGVPR IVFANKMDKI GADFYYSLST LGDRLGANAH PIQIPIGAED DFIGIIDLVT
MKSEIYTNDL GTDIKETVVG SDEFNAELAS LDFNAEEYTE LANEWREKLI EAIADFDEDI
MEKYFAGEEI PEAELKAAIR KATINVDFYP MLAGSAFKNK GVQMMLDAVI DYLPSPLDIP
AIQGVNPDTD EEDERPASDE EPFAALAFKI MTDPFVGRLS FFRVYSGTLD AGSYVLNTSK
GKRERIGRIL QMHANTRKEI QTVYAGDIAA AVGLKNTTTG DSLTDEKAKI ILESIEVPEP
VIQLMVEPKT KADQDKMGVA LQKLAEEDPT FRVETNPETG ETVISGMGEL HLDVLVDRMK
REFKVEANVG APQVAYRETF RAGTSARGFF KRQSGGKGQY GDVWIEFTPN EEGAGFEFEN
AIVGGVVPRE FVPAVEKGLV ETMANGVLAG YPMVDIKAKL YDGSYHDVDS SETAFKVAAS
LAMKEAAKTA KPAILEPMMK VTITVPEENL GDIMGHVTAR RGQVNSMEAH GKSQIVNAFV
PLAEMFGYAT TLRSSTQGRG TFMMVFDHYS DVPKSVQEEI IAKNGRNAD
