EFP_DESAP
ID EFP_DESAP Reviewed; 185 AA.
AC B1I3C0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Daud_1005;
OS Desulforudis audaxviator (strain MP104C).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Candidatus Desulforudis.
OX NCBI_TaxID=477974;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP104C;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL Submitted (OCT-2007) 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; CP000860; ACA59517.1; -; Genomic_DNA.
DR RefSeq; WP_012302103.1; NC_010424.1.
DR AlphaFoldDB; B1I3C0; -.
DR SMR; B1I3C0; -.
DR STRING; 477974.Daud_1005; -.
DR EnsemblBacteria; ACA59517; ACA59517; Daud_1005.
DR KEGG; dau:Daud_1005; -.
DR eggNOG; COG0231; Bacteria.
DR HOGENOM; CLU_074944_0_1_9; -.
DR OMA; WSVVEFQ; -.
DR OrthoDB; 1260763at2; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000008544; 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..185
FT /note="Elongation factor P"
FT /id="PRO_1000096147"
SQ SEQUENCE 185 AA; 20280 MW; 2179EDBC4F6938E2 CRC64;
MISTNEFRTG LTVEVDGDPC QVIEFMHVKP GKGSPFVRAK LKNLRTGAIA ERTFNAGEKL
PRAILERKEM QYLYNDGANY YLMDNETYDQ VGLSAGQLGD GVKYLKENMI INVVYHRGQV
LGVDLPNTVE LTVIETTPGI RGDTASGGSK PAVLETGVVL QVPLFVEEGD VIQVDTRSGA
YIKRA
