EFP1_CHLTR
ID EFP1_CHLTR Reviewed; 185 AA.
AC O84124;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Elongation factor P 1;
DE Short=EF-P 1;
GN Name=efp1; OrderedLocusNames=CT_122;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC67713.1; -; Genomic_DNA.
DR PIR; F71553; F71553.
DR RefSeq; NP_219625.1; NC_000117.1.
DR RefSeq; WP_010725076.1; NC_000117.1.
DR AlphaFoldDB; O84124; -.
DR SMR; O84124; -.
DR STRING; 813.O172_00660; -.
DR EnsemblBacteria; AAC67713; AAC67713; CT_122.
DR GeneID; 884171; -.
DR KEGG; ctr:CT_122; -.
DR PATRIC; fig|272561.5.peg.134; -.
DR HOGENOM; CLU_074944_0_1_0; -.
DR InParanoid; O84124; -.
DR OMA; RWRTTEQ; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..185
FT /note="Elongation factor P 1"
FT /id="PRO_0000094232"
SQ SEQUENCE 185 AA; 20517 MW; DCB00453D6E4D69B CRC64;
MVLSSQLSVG MFISTKDGLY KVVSVSKVSG NKGDTFIKVS LQAAGSDVTV ERNFKAGQEV
KEAQFEPRNL EYLYLEEDKY LFLDLGNYDK IYIPKEIMKD NAMFLKAGVT VFALVHEGTV
FSMELPHFLE LMVAKTDFPG DSLSLSGGAK KALLETGVEV LVPPFVEIGD VIKVDTRTCE
YIQRV