ID   EFP1_CHLMU              Reviewed;         185 AA.
AC   Q9PKR6;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Elongation factor P 1;
DE            Short=EF-P 1;
GN   Name=efp1; OrderedLocusNames=TC_0398;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
CC   -!- FUNCTION: Involved in peptide bond synthesis. Stimulates efficient
CC       translation and peptide-bond synthesis on native or reconstituted 70S
CC       ribosomes in vitro. Probably functions indirectly by altering the
CC       affinity of the ribosome for aminoacyl-tRNA, thus increasing their
CC       reactivity as acceptors for peptidyl transferase (By similarity).
CC       {ECO:0000250}.
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the elongation factor P family. {ECO:0000305}.
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DR   EMBL; AE002160; AAF39255.1; -; Genomic_DNA.
DR   PIR; B81708; B81708.
DR   RefSeq; WP_010230363.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PKR6; -.
DR   SMR; Q9PKR6; -.
DR   STRING; 243161.TC_0398; -.
DR   EnsemblBacteria; AAF39255; AAF39255; TC_0398.
DR   GeneID; 1245750; -.
DR   KEGG; cmu:TC_0398; -.
DR   eggNOG; COG0231; Bacteria.
DR   HOGENOM; CLU_074944_0_1_0; -.
DR   OMA; RWRTTEQ; -.
DR   OrthoDB; 1260763at2; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000000800; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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   PROSITE; PS01275; EFP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; Protein biosynthesis.
FT   CHAIN           1..185
FT                   /note="Elongation factor P 1"
FT                   /id="PRO_0000094227"
SQ   SEQUENCE   185 AA;  20468 MW;  969BD834F4997CE2 CRC64;
     MVLSSQLSVG MFISTKDGLY KVVSVSKVSG SKGDTFIKVA LQAAGSDVVV ERNFKAGQEV
     KEAQFEPRNL EYLYLEEDNY LFLDLGNYEK IYIPKEIMKE NAMFLKAGVT ISALVHEGIV
     FSMELPHFLE LMVSKTDFPG DSLSLSGGAK KALLETGVEV LVPPFVEIGD VIKVDTRTCE
     YIQRV