ID A0A0D4BZ62_9MICC Unreviewed; 704 AA.
AC A0A0D4BZ62;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:AJT41727.1};
GN ORFNames=UM93_09760 {ECO:0000313|EMBL:AJT41727.1};
OS Psychromicrobium lacuslunae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Psychromicrobium.
OX NCBI_TaxID=1618207 {ECO:0000313|EMBL:AJT41727.1, ECO:0000313|Proteomes:UP000061839};
RN [1] {ECO:0000313|EMBL:AJT41727.1, ECO:0000313|Proteomes:UP000061839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHBB 11108 {ECO:0000313|EMBL:AJT41727.1,
RC ECO:0000313|Proteomes:UP000061839};
RX PubMed=25908143;
RA Kiran S., Swarnkar M.K., Pal M., Thakur R., Tewari R., Singh A.K.,
RA Gulati A.;
RT "Complete Genome Sequencing of Protease-Producing Novel Arthrobacter sp.
RT Strain IHBB 11108 Using PacBio Single-Molecule Real-Time Sequencing
RT Technology.";
RL Genome Announc. 3:0-0(2015).
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; CP011005; AJT41727.1; -; Genomic_DNA.
DR RefSeq; WP_045075286.1; NZ_CP011005.1.
DR AlphaFoldDB; A0A0D4BZ62; -.
DR STRING; 1618207.UM93_09760; -.
DR KEGG; ari:UM93_09760; -.
DR PATRIC; fig|1618207.4.peg.1978; -.
DR HOGENOM; CLU_002794_4_1_11; -.
DR OrthoDB; 9801472at2; -.
DR Proteomes; UP000061839; 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}; Reference proteome {ECO:0000313|Proteomes:UP000061839}.
FT DOMAIN 10..290
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 704 AA; 77449 MW; 2F4D0BFB7E619761 CRC64;
MAQDVLTDLT KVRNIGIMAH IDAGKTTTTE RILFYTGVNH KIGETHDGAS TTDWMEQEKE
RGITITSAAV TCFWNKNQIN IIDTPGHVDF TVEVERSLRV LDGAVAVFDG KEGVEPQSET
VWRQADKYNV PRICFVNKMD KLGADFYFTV DTIIGRLGAK PLVMQLPIGA ENDFVGVVDL
LEMRALVWPG DSKGDVTMGA AYEVQEIPAD LQAKAEEYRA ALVETVAESS EELMEKYLEG
EEISIDELKA GIRKMTINSE LYPVFCGSAF KNRGVQPMLD AVIDFLPSPL DVPAMIGHDP
KSEETELTRK PSTEEPFSAL AFKVATHPFF GQLIFIRVYS GEITSGTQVL NSTKGKKERV
GKLFQMHANK EMPVESAHAG HIYAAIGLKD TTTGDTLSDI GSPIVLESMS FPEPVISVAI
EPKTKGDQEK LSTAIQKLSA EDPTFRVNLD EDTGQTIIAG MGELHLDILV DRMRREFRVE
ANVGKPQVAY RETIRRKVEK HDYTHKKQTG GSGQFAKIQI AIEPLDTAEG ALYEFDNKVT
GGRVPREYIP SVDAGIQDAL TDGVLAGYPV VGIKATLLDG AYHDVDSSEM AFKIAGRMAF
KEAARKADPV LLEPMMEVEV RTPEDYMGDV IGDLNARRGQ MQSMEDATGV KVIRALVPLS
GMFGYIGDLR SKTQGRAVYS MQFDSYAEVP KAVADEIIQK ARGE
//