ID   EFP_ACIF2               Reviewed;         186 AA.
AC   B7J6R6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=AFE_0851;
OS   Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS   / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=243159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX   PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA   Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II,
RA   Eisen J.A., Holmes D.S.;
RT   "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT   industrial applications.";
RL   BMC Genomics 9:597-597(2008).
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-33
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-33 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-33 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; CP001219; ACK78221.1; -; Genomic_DNA.
DR   RefSeq; WP_012536394.1; NC_011761.1.
DR   AlphaFoldDB; B7J6R6; -.
DR   SMR; B7J6R6; -.
DR   STRING; 243159.AFE_0851; -.
DR   PaxDb; B7J6R6; -.
DR   EnsemblBacteria; ACK78221; ACK78221; AFE_0851.
DR   GeneID; 66432128; -.
DR   KEGG; afr:AFE_0851; -.
DR   eggNOG; COG0231; Bacteria.
DR   HOGENOM; CLU_074944_1_1_6; -.
DR   OMA; WSVVEFQ; -.
DR   OrthoDB; 1260763at2; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000001362; Chromosome.
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..186
FT                   /note="Elongation factor P"
FT                   /id="PRO_1000117882"
FT   MOD_RES         33
FT                   /note="N6-(3,6-diaminohexanoyl)-5-hydroxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00141"
SQ   SEQUENCE   186 AA;  20767 MW;  E62E1E7ED4AC872D CRC64;
     MKISAFDIRP GNILEYEKGL WRVLKTDFVK PGKGGAFVQV EMKNIETGTK SNTRFRSGEA
     MEKAVVEPRT MQYLYADATG YVFMDNENFE QLILSEDLLE GQTGYLLPNT EIQVNLHNER
     PIGVELPPVV ILEVREAEPS IKGQTATGSY KSAQMETGIT VMVPQFVNAG EKIRVNTVDG
     SYIDRA