ID D7BQS2_STRBB Unreviewed; 707 AA.
AC D7BQS2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Elongation factor G {ECO:0000256|HAMAP-Rule:MF_00054};
DE Short=EF-G {ECO:0000256|HAMAP-Rule:MF_00054};
GN Name=fusA2 {ECO:0000313|EMBL:ADI09289.1};
GN Synonyms=fusA {ECO:0000256|HAMAP-Rule:MF_00054};
GN OrderedLocusNames=SBI_06169 {ECO:0000313|EMBL:ADI09289.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI09289.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI09289.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI09289.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
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; CP002047; ADI09289.1; -; Genomic_DNA.
DR RefSeq; WP_014178749.1; NC_016582.1.
DR AlphaFoldDB; D7BQS2; -.
DR STRING; 749414.SBI_06169; -.
DR KEGG; sbh:SBI_06169; -.
DR PATRIC; fig|749414.3.peg.6360; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_11; -.
DR Proteomes; UP000000377; 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:UP000000377}.
FT DOMAIN 9..296
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 18..25
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 707 AA; 77461 MW; 4854E28D26C12633 CRC64;
MATTSLDLAK VRNIGIMAHI DAGKTTTTER ILFYTGVSYK IGEVHDGAAT MDWMEQEQER
GITITSAATT CHWPLEDVDH TINIIDTPGH VDFTVEVERS LRVLDGAVTV FDGVAGVEPQ
SETVWRQADR YGVPRICFVN KLDRTGAEFH RCVDMIVDRL GAVPLVMQLP IGTEADFKGV
VDLVTMKALV WSAEATKGEM YDTVDIPDTH LDAADEWRGK LLEAVAENDE QMMELYLEGE
EPTVEQLYAA IRRITIASTG TEGSPTITPV FCGTAFKNKG VQPLLDAVVR YLPSPLDIEA
VEGHSVKDPD EVIKRKPSDD EPFAGLAFKI MSDPHLGKLT FVRVYSGRME TGTQVQNSVK
GKKERIGKIY RMHANKREEI DSVGAGDIVA VMGLKQTTTG ETLCDPANPV ILESMDFPAP
VIEVAIEPKS KGDQEKLGVA IQRLAEEDPS FRVKTNEETG QTIIAGMGEL HLDVLVDRMK
REFKVEANVG KPQVAYRETL RKSVDRVDYT HKKQTGGSGQ FAKVQIAIAP LEGDGYEFEN
KVTGGRIPRE YIPSVDAGCQ EAMEFGVLAG YPLTGVKVTL LDGGYHEVDS SEMAFKIAGS
MAFKEAARKA SPALLEPMMK VEVTTPEDYM GDVIGDINSR RGQIQSMEDR SGAKLVTGLV
PLSEMFGYVG DLRSKTSGRA SYSMQFDSYA EVPKSVAEEI IAKAKGE
//
