EFG_HAEIN
ID EFG_HAEIN Reviewed; 700 AA.
AC P43925;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
GN Name=fusA; Synonyms=fus; OrderedLocusNames=HI_0579;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
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DR EMBL; L42023; AAC22237.1; -; Genomic_DNA.
DR PIR; F64078; F64078.
DR RefSeq; NP_438737.1; NC_000907.1.
DR RefSeq; WP_010869011.1; NC_000907.1.
DR PDB; 6B8D; X-ray; 1.78 A; A=1-405.
DR PDBsum; 6B8D; -.
DR AlphaFoldDB; P43925; -.
DR SMR; P43925; -.
DR STRING; 71421.HI_0579; -.
DR PRIDE; P43925; -.
DR EnsemblBacteria; AAC22237; AAC22237; HI_0579.
DR KEGG; hin:HI_0579; -.
DR PATRIC; fig|71421.8.peg.600; -.
DR eggNOG; COG0480; Bacteria.
DR HOGENOM; CLU_002794_4_1_6; -.
DR OMA; AATTCHW; -.
DR PhylomeDB; P43925; -.
DR BioCyc; HINF71421:G1GJ1-592-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..700
FT /note="Elongation factor G"
FT /id="PRO_0000091132"
FT DOMAIN 8..290
FT /note="tr-type G"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 88..92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 10..17
FT /evidence="ECO:0007829|PDB:6B8D"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:6B8D"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:6B8D"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:6B8D"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:6B8D"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:6B8D"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:6B8D"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:6B8D"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:6B8D"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:6B8D"
FT TURN 195..199
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:6B8D"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6B8D"
FT HELIX 212..227
FT /evidence="ECO:0007829|PDB:6B8D"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:6B8D"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:6B8D"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:6B8D"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:6B8D"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:6B8D"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 331..342
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:6B8D"
FT TURN 350..353
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 369..376
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:6B8D"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:6B8D"
SQ SEQUENCE 700 AA; 77264 MW; ADF6F34159A674B0 CRC64;
MARTTPIERY RNIGISAHID AGKTTTTERI LFYTGVSHKI GEVHDGAATM DWMEQEQERG
ITITSAATTA FWSGMSQQFP QHRINVIDTP GHVDFTVEVE RSMRVLDGAV MVYCAVGGVQ
PQSETVWRQA NKYEVPRIAF VNKMDRTGAN FLRVVEQLKT RLGANAIPLQ LPVGAEENFT
GVVDLIKMKA INWNEADQGM TFTYEEVPAN MQADCEEWRQ NLVEAAAEAS EELMEKYLGG
EDLTEEEIKS ALRQRVLANE IILVTCGSAF KNKGVQAMLD AVVEYLPAPT DIPAIKGINP
DETEGERHAS DEEPFSSLAF KIATDPFVGN LTFFRVYSGV INSGDTVLNS VRQKRERFGR
IVQMHANKRE EIKEVRAGDI AAAIGLKDVT TGDTLCAIDA PIILERMEFP EPVISVAVEP
KTKADQEKMG LALGRLAQED PSFRVHTDEE SGETIISGMG ELHLDIIVDR MKREFKVEAN
IGKPQVSYRE TIRTRVNDVE GKHAKQSGGR GQYGHVVIDL YPLDPEGPGY EFVNEIKGGV
IPGEYIPAVD KGIQEQLKSG PLAGYPVVDL GVRLHFGSYH DVDSSELAFK LAASLAFKAA
FSKANPVLLE PIMKVEVETP PEYVGDVIGD LSRRRAMVNG QEANEFVVKI YAEVPLSEMF
GYATDLRSQT QGRASYSMEP LKYAEAPTSV AAAVIEARKK
