EFP_BUCMP
ID EFP_BUCMP Reviewed; 187 AA.
AC O51834;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Elongation factor P {ECO:0000255|HAMAP-Rule:MF_00141};
DE Short=EF-P {ECO:0000255|HAMAP-Rule:MF_00141};
DE Flags: Fragment;
GN Name=efp {ECO:0000255|HAMAP-Rule:MF_00141};
OS Buchnera aphidicola subsp. Myzus persicae (Myzus persicae primary
OS endosymbiont).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=98795;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9420234; DOI=10.1128/jvi.72.1.358-365.1998;
RA Hogenhout S.A., van der Wilk F., Verbeek M., Goldbach R.W.,
RA van den Heuvel J.F.J.M.;
RT "Potato leafroll virus binds to the equatorial domain of the aphid
RT endosymbiotic GroEL homolog.";
RL J. Virol. 72:358-365(1998).
CC -!- FUNCTION: Involved in peptide bond synthesis. Alleviates ribosome
CC stalling that occurs when 3 or more consecutive Pro residues or the
CC sequence PPG is present in a protein, possibly by augmenting the
CC peptidyl transferase activity of the ribosome. Modification of Lys-34
CC is required for alleviation. {ECO:0000255|HAMAP-Rule:MF_00141}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000255|HAMAP-Rule:MF_00141}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00141}.
CC -!- PTM: May be beta-lysylated on the epsilon-amino group of Lys-34 by the
CC combined action of EpmA and EpmB, and then hydroxylated on the C5
CC position of the same residue by EpmC (if this protein is present).
CC Lysylation is critical for the stimulatory effect of EF-P on peptide-
CC bond formation. The lysylation moiety may extend toward the
CC peptidyltransferase center and stabilize the terminal 3-CCA end of the
CC tRNA. Hydroxylation of the C5 position on Lys-34 may allow additional
CC potential stabilizing hydrogen-bond interactions with the P-tRNA.
CC {ECO:0000255|HAMAP-Rule:MF_00141}.
CC -!- SIMILARITY: Belongs to the elongation factor P family.
CC {ECO:0000255|HAMAP-Rule:MF_00141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF003957; AAC04239.1; -; Genomic_DNA.
DR AlphaFoldDB; O51834; -.
DR SMR; O51834; -.
DR UniPathway; UPA00345; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR CDD; cd04470; S1_EF-P_repeat_1; 1.
DR CDD; cd05794; S1_EF-P_repeat_2; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 2.
DR HAMAP; MF_00141; EF_P; 1.
DR InterPro; IPR015365; Elong-fact-P_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR020599; Transl_elong_fac_P/YeiP.
DR InterPro; IPR013185; Transl_elong_KOW-like.
DR InterPro; IPR001059; Transl_elong_P/YeiP_cen.
DR InterPro; IPR013852; Transl_elong_P/YeiP_CS.
DR InterPro; IPR011768; Transl_elongation_fac_P.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR30053; PTHR30053; 1.
DR Pfam; PF01132; EFP; 1.
DR Pfam; PF08207; EFP_N; 1.
DR Pfam; PF09285; Elong-fact-P_C; 1.
DR PIRSF; PIRSF005901; EF-P; 1.
DR SMART; SM01185; EFP; 1.
DR SMART; SM00841; Elong-fact-P_C; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
DR TIGRFAMs; TIGR00038; efp; 1.
DR PROSITE; PS01275; EFP; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; Hydroxylation; Protein biosynthesis.
FT CHAIN 1..>187
FT /note="Elongation factor P"
FT /id="PRO_0000094218"
FT MOD_RES 34
FT /note="N6-(3,6-diaminohexanoyl)-5-hydroxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00141"
FT NON_TER 187
SQ SEQUENCE 187 AA; 21535 MW; 9C803DCA4EEEA025 CRC64;
MRVYHSNNFR SGCKIIFENE PYLIESSEFV KPGKGQAFVR VKLRKLLTRQ LIEKTFKSTD
YLEIADVIEH TLCYLYNDGF FWYFINNNTF EELSVEKKII GIQKKWLLEQ DTCIVTLWNN
KPILVTPNTF VEIKVIETDA TLKGDTINTG VTKLAILSTG AIVRVPLFIQ VGSLIKVDTR
SGEYVSR