ID A0A0K2GYZ2_9CORY Unreviewed; 710 AA.
AC A0A0K2GYZ2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ORFNames=CLAC_01930 {ECO:0000313|EMBL:ALA66691.1};
OS Corynebacterium lactis RW2-5.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1408189 {ECO:0000313|EMBL:ALA66691.1, ECO:0000313|Proteomes:UP000058446};
RN [1] {ECO:0000313|EMBL:ALA66691.1, ECO:0000313|Proteomes:UP000058446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RW2-5 {ECO:0000313|EMBL:ALA66691.1,
RC ECO:0000313|Proteomes:UP000058446};
RA Ruckert C., Albersmeier A., Lipski A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium lactis DSM 45799(T), isolated
RT from raw cow milk.";
RL Submitted (OCT-2013) 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}.
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DR EMBL; CP006841; ALA66691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K2GYZ2; -.
DR STRING; 1408189.CLAC_01930; -.
DR KEGG; clw:CLAC_01930; -.
DR PATRIC; fig|1408189.4.peg.384; -.
DR OrthoDB; 9801472at2; -.
DR Proteomes; UP000058446; 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; 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}.
FT DOMAIN 13..289
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 22..29
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 86..90
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 140..143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 710 AA; 78135 MW; 6E9FE75EDCA3F8E9 CRC64;
MAEGALPVKK DLHKVRNIGI MAHIDAGKTT TTERILFYTG INRKVGETHD GASTTDWMEQ
EKERGITITS AAVTCFWNDN QINIIDTPGH VDFTVEVERS LRVLDGAVAV FDGKEGVEPQ
SEQVWRQAQK YDVPRICFVN KMDKLGADFE YTVGTIIDRL GAKPLVMQLP IGAEDDFEGV
IDLLEMKAHV WPGKVEIGTP ANIEEIPAEL ADKAAEYREK LIETVAESDE ELMEKYFGGE
ELTMEEIKGA IRKMVLNSEI YPVYCGSAYK NKGVEPLLDA VIDFLPNPLD IGEVHGHQMG
AEDVGMTRKP SKDEPFSALA FKIAAHPFFG KLTFVRVYSG RVEPGQQVLN STKDKKERVG
KLFQMHANKE NPVDEAVAGN IYAFIGLKDT TTGDTLCAQD APIVLESMSF PDPVISVAIE
PKSKADQEKL GTAIQRLAEE DPTFTVKLDE ETGQTVIGGM GELHLDVLVD RMKREFKVEA
NVGAPQVAYR ETIRKPVEKY EYTHKKQTGG SGQFARVIIA LEPYAPSADE LEEGESATYL
FANEVTGGRV PKEYIPSVDA GIQDAMQYGT VAGFPLVNIK ATLLDGAYHE VDSSEMAFKI
AGQQALKEAV QKAKPVLLEP MMAVEVITPE EYMGEVIGDI NSRRGQVNSM EDRTGVKAVK
ALVPLSEMFG YVGDLRSKTQ GRANYTMIFD SYAEVPSSVA EEIIASRNGN
//
