ID   EFP_VIBA3               Reviewed;         188 AA.
AC   B7VHR3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=VS_0244;
OS   Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=575788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LGP32;
RA   Mazel D., Le Roux F.;
RT   "Vibrio splendidus str. LGP32 complete genome.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; FM954972; CAV17275.1; -; Genomic_DNA.
DR   RefSeq; WP_009847919.1; NC_011753.2.
DR   AlphaFoldDB; B7VHR3; -.
DR   SMR; B7VHR3; -.
DR   STRING; 575788.VS_0244; -.
DR   EnsemblBacteria; CAV17275; CAV17275; VS_0244.
DR   GeneID; 50231218; -.
DR   KEGG; vsp:VS_0244; -.
DR   eggNOG; COG0231; Bacteria.
DR   HOGENOM; CLU_074944_0_0_6; -.
DR   OMA; WSVVEFQ; -.
DR   OrthoDB; 1260763at2; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000009100; Chromosome 1.
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;
KW   Reference proteome.
FT   CHAIN           1..188
FT                   /note="Elongation factor P"
FT                   /id="PRO_1000123038"
FT   MOD_RES         34
FT                   /note="N6-(3,6-diaminohexanoyl)-5-hydroxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00141"
SQ   SEQUENCE   188 AA;  20585 MW;  E52C1DE1A1280AF3 CRC64;
     MASVSTNEFK GGLKFMLDNE PCAIIDNEYV KPGKGQAFNR VKLRKLLSGK VLEKTFKSGE
     SFELADVVDV ELGYLYNDGE FYHFMNNETF EQIAADVKAV ADSAKWLVEN DVCTLTLWND
     NPITVTPPNF VEIEVTETDP GLKGDTQGTG GKPATLATGA VVRVPLFIAI GEVVKVDTRT
     GEYVGRVK