ID   EFP_UREPA               Reviewed;         188 AA.
AC   Q9PQJ3;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Elongation factor P;
DE            Short=EF-P;
GN   Name=efp; OrderedLocusNames=UU298;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL   Nature 407:757-762(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; AF222894; AAF30707.1; -; Genomic_DNA.
DR   RefSeq; WP_006688853.1; NC_002162.1.
DR   AlphaFoldDB; Q9PQJ3; -.
DR   SMR; Q9PQJ3; -.
DR   STRING; 273119.UU298; -.
DR   EnsemblBacteria; AAF30707; AAF30707; UU298.
DR   GeneID; 29672456; -.
DR   KEGG; uur:UU298; -.
DR   eggNOG; COG0231; Bacteria.
DR   HOGENOM; CLU_074944_2_1_14; -.
DR   OMA; WSVVEFQ; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000000423; 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; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..188
FT                   /note="Elongation factor P"
FT                   /id="PRO_0000094363"
SQ   SEQUENCE   188 AA;  21221 MW;  6EE4A873CF7F7E15 CRC64;
     MATIIQAKDL RAGHTFLYKG NIYQVIENSF NKTAMREGIV KCKVKNLRTG AITIEVLTGE
     KLEQAVIEKS KMTFSYDDGS GYVFMDNDTY EQISIPYSQL SWEKNFIEEG TEVSVMRYDG
     ELMGVSLPDQ LVVTIIEAEE AVQGNSVQNA TKRAWLESKW EFQVPQFIKS GEKVIINPSN
     GQYVGRAK