EFG_BARHE
ID EFG_BARHE Reviewed; 694 AA.
AC Q8KQB3;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Elongation factor G {ECO:0000255|HAMAP-Rule:MF_00054};
DE Short=EF-G {ECO:0000255|HAMAP-Rule:MF_00054};
GN Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=BH10540;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12140235; DOI=10.1093/oxfordjournals.molbev.a004184;
RA Amiri H., Alsmark C.M., Andersson S.G.E.;
RT "Proliferation and deterioration of Rickettsia palindromic elements.";
RL Mol. Biol. Evol. 19:1234-1243(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; AY099293; AAM92279.1; -; Genomic_DNA.
DR EMBL; BX897699; CAF27845.1; -; Genomic_DNA.
DR RefSeq; WP_011180915.1; NZ_LRIJ02000001.1.
DR AlphaFoldDB; Q8KQB3; -.
DR SMR; Q8KQB3; -.
DR STRING; 283166.BH10540; -.
DR PaxDb; Q8KQB3; -.
DR PRIDE; Q8KQB3; -.
DR EnsemblBacteria; CAF27845; CAF27845; BH10540.
DR GeneID; 64157264; -.
DR KEGG; bhe:BH10540; -.
DR eggNOG; COG0480; Bacteria.
DR OMA; AATTCHW; -.
DR Proteomes; UP000000421; 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..694
FT /note="Elongation factor G"
FT /id="PRO_0000091073"
FT DOMAIN 8..287
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 86..90
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT BINDING 140..143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ SEQUENCE 694 AA; 76333 MW; 8C90C4C3B856B3BE CRC64;
MAREYKIEDY RNFGIMAHID AGKTTMTERI LFYTGKNHKI GETHDGASTM DWMEQEQERG
ITITSAATTT FWEGRDGRKR RFNIIDTPGH VDFTIEVERS LRVLDGAIAL LDANAGVEPQ
TETVWRQAEK YRVPRMVFVN KMDKIGADFY RSVEMVGSRL GAKALVLQLP IGAENDFEGV
VDLIEMQALR WDGSIGASAT VGEIPSGLKE KAEEYREKLV EMAVEVDEAA TEAYLEGVMP
TNEQLVALIR KGTVEVQFHP VLCGTAFKNK GVQPLLDAVV SYLPSPVDVP AISGVDVKTE
GETTRESSDD APLSMLAFKI MNDPFVGSLT FCRIYSGKVQ KGISLENTVK RKKERLGRML
QMHSNSREDI EEAFAGDIVA LAGLKETTTG DTLCDPLKPV ILERMEFPEP VIEIAIEPKT
KADQEKMGIA LNRLAAEDPS FRVKSDEESG QTIIAGMGEL HLDIIVDRMR REFKVEANVG
QPQVAYRESI TKIAEIDYTH KKQSGGAGQF ARVKIIFEPH DGDDFIFESK IVGGAVPKEY
IPGVQKGIES VMGSGPLAGF PMLGVKATLV DGGYHDVDSS VLAFEIAARA AFRDGAKKAG
AQLLEPIMKV EVVTPEDYVG DVIGDLNSRR GQISGTEARG IATVVNAMVP LANMFGYVNS
LRSMSQGRAQ YTMQFDHYEP VPSAVALEIQ KKYA
