EFP_SOLM1
ID EFP_SOLM1 Reviewed; 185 AA.
AC C4XT92;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=DMR_23980;
OS Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1)
OS (Desulfovibrio magneticus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Solidesulfovibrio.
OX NCBI_TaxID=573370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700980 / DSM 13731 / RS-1;
RX PubMed=19675025; DOI=10.1101/gr.088906.108;
RA Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N.,
RA Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H.,
RA Matsunaga T.;
RT "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed
RT common gene clusters in magnetotactic bacteria.";
RL Genome Res. 19:1801-1808(2009).
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; AP010904; BAH75889.1; -; Genomic_DNA.
DR RefSeq; WP_015861069.1; NC_012796.1.
DR AlphaFoldDB; C4XT92; -.
DR SMR; C4XT92; -.
DR STRING; 573370.DMR_23980; -.
DR PRIDE; C4XT92; -.
DR EnsemblBacteria; BAH75889; BAH75889; DMR_23980.
DR KEGG; dma:DMR_23980; -.
DR eggNOG; COG0231; Bacteria.
DR HOGENOM; CLU_074944_0_1_7; -.
DR OMA; WSVVEFQ; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000009071; 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.
FT CHAIN 1..185
FT /note="Elongation factor P"
FT /id="PRO_1000203265"
SQ SEQUENCE 185 AA; 20602 MW; A2293F51678C92CE CRC64;
MLSTTDFRRG LKIEMDGVPY EIVDFLHVKP GKGGAFIRTK LKNMINGRVV ENTFRSGEKM
VKPDLESKDM QYLYRESEDF VFMDMESYEQ MHAGAAQLGE KGGYLKDGME LKMLLYKGQP
LDIDLPASVV LQVAETEPGV KGDTVSGATK PAQLETGITV NVPLFVNIGD RIKVDTRSGD
YIGRE
