EFP_FRATW
ID EFP_FRATW Reviewed; 189 AA.
AC A4J019;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Elongation factor P {ECO:0000255|HAMAP-Rule:MF_00141};
DE Short=EF-P {ECO:0000255|HAMAP-Rule:MF_00141};
GN Name=efp {ECO:0000255|HAMAP-Rule:MF_00141}; OrderedLocusNames=FTW_1860;
OS Francisella tularensis subsp. tularensis (strain WY96-3418).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=418136;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WY96-3418;
RX PubMed=17895988; DOI=10.1371/journal.pone.0000947;
RA Beckstrom-Sternberg S.M., Auerbach R.K., Godbole S., Pearson J.V.,
RA Beckstrom-Sternberg J.S., Deng Z., Munk C., Kubota K., Zhou Y., Bruce D.,
RA Noronha J., Scheuermann R.H., Wang A., Wei X., Wang J., Hao J.,
RA Wagner D.M., Brettin T.S., Brown N., Gilna P., Keim P.S.;
RT "Complete genomic characterization of a pathogenic A.II strain of
RT Francisella tularensis subspecies tularensis.";
RL PLoS ONE 2:E947-E947(2007).
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}.
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DR EMBL; CP000608; ABO47520.1; -; Genomic_DNA.
DR RefSeq; WP_003014194.1; NC_009257.1.
DR AlphaFoldDB; A4J019; -.
DR SMR; A4J019; -.
DR KEGG; ftw:FTW_1860; -.
DR HOGENOM; CLU_074944_0_0_6; -.
DR OMA; WSVVEFQ; -.
DR UniPathway; UPA00345; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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..189
FT /note="Elongation factor P"
FT /id="PRO_1000010750"
FT MOD_RES 34
FT /note="N6-(3,6-diaminohexanoyl)-5-hydroxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00141"
SQ SEQUENCE 189 AA; 20903 MW; F20115760ACE0CBC CRC64;
MASYSTNEFK GGLKVLIDGN PMVIVENEFV KPGKGQAFNR VKLKNLLNDR VVEKTFKSGE
SVEAADVEEL TTVYSYFDGD SYVFMHPETF EQYMVSEEAL GETKKWLKDQ DEYQVILFNG
QPISIIAANF VNLEIIETDP GLKGDTAGTG GKPATLSTGA VVRVPLFVQT GEIIKVDTRT
STYVSRVKD