ID   EFP_NATTJ               Reviewed;         188 AA.
AC   B2A549;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=Nther_1717;
OS   Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS   JW/NM-WN-LF).
OC   Bacteria; Firmicutes; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC   Natranaerobius.
OX   NCBI_TaxID=457570;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT   "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT   LF.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC       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   -!- SIMILARITY: Belongs to the elongation factor P family.
CC       {ECO:0000255|HAMAP-Rule:MF_00141}.
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DR   EMBL; CP001034; ACB85291.1; -; Genomic_DNA.
DR   RefSeq; WP_012448158.1; NC_010718.1.
DR   AlphaFoldDB; B2A549; -.
DR   SMR; B2A549; -.
DR   STRING; 457570.Nther_1717; -.
DR   EnsemblBacteria; ACB85291; ACB85291; Nther_1717.
DR   KEGG; nth:Nther_1717; -.
DR   eggNOG; COG0231; Bacteria.
DR   HOGENOM; CLU_074944_0_1_9; -.
DR   OMA; WSVVEFQ; -.
DR   OrthoDB; 1260763at2; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000001683; 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; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..188
FT                   /note="Elongation factor P"
FT                   /id="PRO_1000117902"
SQ   SEQUENCE   188 AA;  21145 MW;  008571C7EA4BF27F CRC64;
     MITSNDFKNG MTIEVDGEVY SIVEFQHVKP GKGAAFVRTK LRHMKSGNVS EKTFRAGEKV
     KRAHLEEREM QFLYAAGDMY NFMDTESFEQ YTLTKDQLED KTQFIKENMI ITVLFHNGEE
     ISIELPVFVE LAVSETEPGV KGDTASGGSK PATLETGATV NVPFFINEGD IIKVDTRTSE
     YIERVKGE