ID   LEPA_STRP8              Reviewed;         174 AA.
AC   Q8P173;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Putative elongation factor 4;
DE            Short=EF-4;
DE            EC=3.6.5.n1;
DE   AltName: Full=Ribosomal back-translocase LepA homolog;
GN   Name=lepA; OrderedLocusNames=spyM18_1028;
OS   Streptococcus pyogenes serotype M18 (strain MGAS8232).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=186103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGAS8232;
RX   PubMed=11917108; DOI=10.1073/pnas.062526099;
RA   Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S.,
RA   Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D.,
RA   Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A.,
RA   Veasy L.G., Musser J.M.;
RT   "Genome sequence and comparative microarray analysis of serotype M18 group
RT   A Streptococcus strains associated with acute rheumatic fever outbreaks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002).
CC   -!- FUNCTION: Required for accurate and efficient protein synthesis under
CC       certain stress conditions. May act as a fidelity factor of the
CC       translation reaction, by catalyzing a one-codon backward translocation
CC       of tRNAs on improperly translocated ribosomes. Back-translocation
CC       proceeds from a post-translocation (POST) complex to a pre-
CC       translocation (PRE) complex, thus giving elongation factor G a second
CC       chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-
CC       dependent manner (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.n1;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. LepA
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. The N-terminal region is
CC       truncated when compared to orthologs. {ECO:0000305}.
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DR   EMBL; AE009949; AAL97661.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8P173; -.
DR   SMR; Q8P173; -.
DR   KEGG; spm:spyM18_1028; -.
DR   HOGENOM; CLU_009995_1_1_9; -.
DR   OMA; FILRTEE; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.2570; -; 1.
DR   InterPro; IPR006297; EF-4.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR038363; LepA_C_sf.
DR   InterPro; IPR013842; LepA_CTD.
DR   PANTHER; PTHR43512; PTHR43512; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF06421; LepA_C; 1.
DR   SUPFAM; SSF54980; SSF54980; 1.
PE   5: Uncertain;
KW   Cell membrane; GTP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..174
FT                   /note="Putative elongation factor 4"
FT                   /id="PRO_0000176383"
SQ   SEQUENCE   174 AA;  20010 MW;  1C2F7A3B5DA85139 CRC64;
     MKQTLDYIDD NRVNVIYQIP LAEIVFDFFD KLKSSTRGYA SFDYDMSEYR RSQLVKMDIL
     LNGDKVDALS FIVHKEFAYE RGKIIVEKLK KIIPRQQFEV PIQAAIGQKI VARSDIKALR
     KNVLAKCYGG DVSRKRKLLE KQKAGKKRMK AIGSVEVPQE AFLSVLSMDE DAKK