EFG1_BORPA
ID EFG1_BORPA Reviewed; 700 AA.
AC Q7W2F8;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Elongation factor G 1 {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-G 1 {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusA1 {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=BPP0026;
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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:0000255|HAMAP-
CC Rule:MF_00054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00054}.
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DR EMBL; BX640423; CAE39767.1; -; Genomic_DNA.
DR RefSeq; WP_010927267.1; NC_002928.3.
DR AlphaFoldDB; Q7W2F8; -.
DR SMR; Q7W2F8; -.
DR EnsemblBacteria; CAE39767; CAE39767; BPP0026.
DR KEGG; bpa:BPP0026; -.
DR HOGENOM; CLU_002794_4_1_4; -.
DR OMA; MDDMVGG; -.
DR Proteomes; UP000001421; 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; 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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..700
FT /note="Elongation factor G 1"
FT /id="PRO_0000091084"
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:0000255|HAMAP-Rule:MF_00054"
FT BINDING 88..92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 700 AA; 77114 MW; CB9C645DC6C7BCF8 CRC64;
MARKTPIERY RNIGISAHID AGKTTTTERI LFYTGVNHKL GETHDGSATM DWMEQEQERG
ITITSAATTA FWRGMAGNYP EYRINIIDTP GHVDFTIEVE RSMRVLDGAC MVYCAVGGVQ
PQSETVWRQA NKYGVPRLAF VNKMDRTGAN FFKVYDQLKT RLRANPVPIV IPIGAEDSFT
GVVDLVKMKA IIWDEASQGT KFEYGDIPAE LEGTANEWRE KLVEAAAESS EELMNKYLET
GSLDEDDINV ALRQRTIAGE IQPMLCGTAF KNKGVQRMLD AVIDYLPSPA DIPPVDGQDD
DGNPIKRSAD DAEKFSALAF KLMSDPFVGQ LTFVRVYSGV LKSGDTVYNP IKGKKERIGR
LLQMHANNRE EIKEVLAGDI AAVVGLKDVT TGETLCDIDS HILLERMEFP EPVISQAVEP
KSKADQEKMG LALSRLAQED PSFRVRSDEE SGQTIISGMG ELHLEILVDR MRREFGVEAN
VGKPQVAYRE TIRKNCDEVE GKFVKQSGGR GQYGHVVLKL EPLPPGGGYE FVDAIKGGVV
PREYIPAVDK GIQETLPAGI LAGYPVVDVK ATLFFGSYHD VDSNENAFKM AASMAFKEGM
RRASPVLLEP MMAVEVETPE DYAGTVMGDL SSRRGMVQGM DDIVGGGKTI KAEVPLAEMF
GYATNLRSLT QGRATYTMEF KHYAEAPKNV ADEVIAARGK
