ID   EFG_NEIGO               Reviewed;         226 AA.
AC   P48862;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
DE   Flags: Fragment;
GN   Name=fusA;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MS11;
RX   PubMed=8828215; DOI=10.1099/00221287-142-9-2481;
RA   Porcella S.F., Belland R.J., Judd R.C.;
RT   "Identification of an EF-Tu protein that is periplasm-associated and
RT   processed in Neisseria gonorrhoeae.";
RL   Microbiology 142:2481-2489(1996).
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 GTP-binding elongation factor family. EF-
CC       G/EF-2 subfamily. {ECO:0000305}.
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DR   EMBL; L36380; AAB41516.1; -; Genomic_DNA.
DR   PIR; T10167; T10167.
DR   AlphaFoldDB; P48862; -.
DR   SMR; P48862; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   CDD; cd03713; EFG_mtEFG_C; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR035649; EFG_V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF54980; SSF54980; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           <1..226
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091166"
FT   NON_TER         1
SQ   SEQUENCE   226 AA;  24902 MW;  9F20C8CAFD4B9D53 CRC64;
     KFGVEANIGA PQVAYRETIR KAVKAEYKHA KQSGGKGQYG HVVIEMEPME PGGEGYEFID
     EIKGGVIPRE FIRLSIKVSA ILAYRYRCRL SVVDVRIRLV FGSYHDVDSS QLAFELAASQ
     AFKEGMRQAS PALLEPIMAV EVETPEEYMG DVMGDLNRRR GVVLGMDDDG IGGKKVRAEV
     PLAEMFGYST DLRSATQGRA TYSMEFKKYS EAPAHIAAAV TEARKG