ID A0A1L7CJY2_CORFL Unreviewed; 711 AA.
AC A0A1L7CJY2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Elongation factor G {ECO:0000256|HAMAP-Rule:MF_00054};
DE Short=EF-G {ECO:0000256|HAMAP-Rule:MF_00054};
GN Name=fusA {ECO:0000256|HAMAP-Rule:MF_00054,
GN ECO:0000313|EMBL:APT86098.1};
GN ORFNames=CFLV_02085 {ECO:0000313|EMBL:APT86098.1}, F4V60_02005
GN {ECO:0000313|EMBL:KAA8724607.1};
OS Corynebacterium flavescens.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=28028 {ECO:0000313|EMBL:APT86098.1, ECO:0000313|Proteomes:UP000185479};
RN [1] {ECO:0000313|EMBL:APT86098.1, ECO:0000313|Proteomes:UP000185479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OJ8 {ECO:0000313|EMBL:APT86098.1,
RC ECO:0000313|Proteomes:UP000185479};
RA Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium flavescens OJ8(T)(=DSM
RT 20296(T)), isolated from cheese.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAA8724607.1, ECO:0000313|Proteomes:UP000322697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 28791T {ECO:0000313|EMBL:KAA8724607.1,
RC ECO:0000313|Proteomes:UP000322697};
RA Pineiro-Iglesias B., Tunovic T., Unosson C., Inganas E., Ohlen M.,
RA Cardew S., Jensie-Markopoulos S., Salva-Serra F., Jaen-Luchoro D.,
RA Karlsson R., Svensson-Stadler L., Chun J., Moore E.;
RT "Draft genome sequence of various Type strains from the CCUG.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00024731,
CC ECO:0000256|HAMAP-Rule:MF_00054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|ARBA:ARBA00005870, ECO:0000256|HAMAP-
CC Rule:MF_00054}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009246; APT86098.1; -; Genomic_DNA.
DR EMBL; VXKK01000015; KAA8724607.1; -; Genomic_DNA.
DR RefSeq; WP_075729096.1; NZ_VXKK01000015.1.
DR AlphaFoldDB; A0A1L7CJY2; -.
DR STRING; 28028.CFLV_02085; -.
DR GeneID; 82879510; -.
DR KEGG; cfc:CFLV_02085; -.
DR OrthoDB; 9801472at2; -.
DR Proteomes; UP000185479; Chromosome.
DR Proteomes; UP000322697; Unassembled WGS sequence.
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; cd01886; EF-G; 1.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR CDD; cd04088; EFG_mtEFG_II; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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; IPR047872; EFG_IV.
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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_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 NCBIfam; TIGR00484; EF-G; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
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; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00054};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00054}; Reference proteome {ECO:0000313|Proteomes:UP000185479}.
FT DOMAIN 10..286
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 83..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 137..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 711 AA; 78098 MW; CE533D8BA7303398 CRC64;
MAQQVLKDLH KVRNIGIMAH IDAGKTTTTE RILFYTGINR KVGETHDGAS TTDWMEQEKE
RGITITSAAV TCFWDGNQIN IIDTPGHVDF TVEVERSLRV LDGAVAVFDG KEGVEPQSEQ
VWRQAAKYDV PRICFVNKMD KLGADFYFTV QTIIDRLGAK PLVLQLPIGA EDDFDGVVDL
LTMRAITWRG KVETGAEPTI EEIPADLKDK ADEYREKLLE TVAESDEALM EKYFGGEELT
LDEIKAAIRK MTINSELYPV LCGTAYRNKG VQPLLDAVVD FLPSPLDIGE VIGHAVGDED
KELTRKPSID SPFSALSFKI AAQPFFGQLN FIRVYSGQVL PGTEVLNSTK GKKERIGKLF
QMHANKENPV EQADAGNIYA VIGLKETTTG DTLCDKNDPI ILESMDFPDP VIKVSIEPKT
KADQEKLGTA IQKLAAEDPT FTVELDDETG QTVIGGMGEL HLDVLVDRMK REFKVEANIG
NPQVAYRETI RKTVQSLDYT HKKQTGGSGQ FAKVIVTIEP YNPDPETLEE GESATYKFVN
AVTGGRIPRE YIPSVDAGIQ DAMQYGYLAG FPLVNIKATL EDGAYHDVDS SEMAFKLAGS
QVLKEAVAKA KPVLLEPVMA VEVVTPEEYM GTVNGDISSR RGQVYAMEDR SGAKVVKAKV
PLSEMFGYIG DLRSSTAGRA NFSMVFDSYA EVPASVSAAI IEERTGTKGH H
//
