ID   EFP_COXBN               Reviewed;         188 AA.
AC   A9KEY9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=CBUD_0045;
OS   Coxiella burnetii (strain Dugway 5J108-111).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=434922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dugway 5J108-111;
RX   PubMed=19047403; DOI=10.1128/iai.01141-08;
RA   Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA   Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA   Heinzen R.A.;
RT   "Comparative genomics reveal extensive transposon-mediated genomic
RT   plasticity and diversity among potential effector proteins within the genus
RT   Coxiella.";
RL   Infect. Immun. 77:642-656(2009).
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; CP000733; ABS78254.1; -; Genomic_DNA.
DR   RefSeq; WP_005772139.1; NC_009727.1.
DR   AlphaFoldDB; A9KEY9; -.
DR   SMR; A9KEY9; -.
DR   EnsemblBacteria; ABS78254; ABS78254; CBUD_0045.
DR   KEGG; cbd:CBUD_0045; -.
DR   HOGENOM; CLU_074944_0_0_6; -.
DR   OMA; WSVVEFQ; -.
DR   OrthoDB; 1260763at2; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000008555; 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.
FT   CHAIN           1..188
FT                   /note="Elongation factor P"
FT                   /id="PRO_1000076511"
FT   MOD_RES         34
FT                   /note="N6-(3,6-diaminohexanoyl)-5-hydroxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00141"
SQ   SEQUENCE   188 AA;  21045 MW;  CA879258AFAE41E3 CRC64;
     MATHSTNEFR GGLKVMVDGD PCSIIDNEFV KPGKGQAFNR VKFRNLKTGR VLERTFKSGE
     TLPAADVVEV EMQYLYNDGE FWHFMTSENY EQHAASKEAV AEAKQWLKEE ALCMVTMWNG
     VPLSVEPPNF VELKITETEP GVRGDTATGG TKRAKLETGA VVRVPLFLNE GEIIKVDTRR
     GEYVSRAK