EFP_NOSS1
ID EFP_NOSS1 Reviewed; 185 AA.
AC Q44247;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Elongation factor P;
DE Short=EF-P;
GN Name=efp; OrderedLocusNames=all5058;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8102363; DOI=10.1128/jb.175.16.5268-5272.1993;
RA Gornicki P., Scappino L.A., Haselkorn R.;
RT "Genes for two subunits of acetyl coenzyme A carboxylase of Anabaena sp.
RT strain PCC 7120: biotin carboxylase and biotin carboxyl carrier protein.";
RL J. Bacteriol. 175:5268-5272(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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; L14863; AAA74627.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB76757.1; -; Genomic_DNA.
DR PIR; AB2438; AB2438.
DR RefSeq; WP_010999184.1; NZ_RSCN01000014.1.
DR AlphaFoldDB; Q44247; -.
DR SMR; Q44247; -.
DR STRING; 103690.17134196; -.
DR EnsemblBacteria; BAB76757; BAB76757; BAB76757.
DR KEGG; ana:all5058; -.
DR eggNOG; COG0231; Bacteria.
DR OMA; WSVVEFQ; -.
DR OrthoDB; 1260763at2; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000002483; 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_0000094188"
SQ SEQUENCE 185 AA; 20496 MW; F5F32A12CF106182 CRC64;
MISSNDFRPG VSIVLDGSVW RVIDFLHVKP GKGSAFVRTT LKNVQSGKVL EKTFRAGETV
PQATLEKITM QHTYKEGDEF VFMDMESYEE GRLSAAQIGD RVKYLKEGME VNVIRWGEQV
LEVELANSVV LEVIQTDPGV KGDTATGGTK PAIVETGATV MVPLFISQGE RIKIDTRDDK
YLGRE