EFP1_GEOSL
ID EFP1_GEOSL Reviewed; 187 AA.
AC Q74FY7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Elongation factor P 1 {ECO:0000255|HAMAP-Rule:MF_00141};
DE Short=EF-P 1 {ECO:0000255|HAMAP-Rule:MF_00141};
GN Name=efp1 {ECO:0000255|HAMAP-Rule:MF_00141}; Synonyms=efp-1;
GN OrderedLocusNames=GSU0465;
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA Lovley D.R., Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
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; AE017180; AAR33797.1; -; Genomic_DNA.
DR RefSeq; NP_951524.1; NC_002939.5.
DR RefSeq; WP_010941133.1; NC_002939.5.
DR AlphaFoldDB; Q74FY7; -.
DR SMR; Q74FY7; -.
DR STRING; 243231.GSU0465; -.
DR EnsemblBacteria; AAR33797; AAR33797; GSU0465.
DR KEGG; gsu:GSU0465; -.
DR PATRIC; fig|243231.5.peg.463; -.
DR eggNOG; COG0231; Bacteria.
DR HOGENOM; CLU_074944_0_1_7; -.
DR InParanoid; Q74FY7; -.
DR OMA; LYRMRMY; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
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..187
FT /note="Elongation factor P 1"
FT /id="PRO_0000094253"
SQ SEQUENCE 187 AA; 21059 MW; F6F9EB8A144E9049 CRC64;
MLTTSDFKRG LVIKLDNSPC LILDVHFQSP SARGASTMVK TRYRNLLTGQ VLDKTFRSGD
KVEEADFERH KGQYLYADGD RGVFMDMETY EQFEMDAESF QVIQPYLLDG TEVVLGLFQE
RLVSVDPPQV VELTITDTPP VIKNATATAQ TKEATLETGL TLQVPPYLEV GEKIKVDTRD
CRFISRA