EFP_STRPC
ID EFP_STRPC Reviewed; 185 AA.
AC Q1JK85;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 96.
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};
GN OrderedLocusNames=MGAS9429_Spy1551;
OS Streptococcus pyogenes serotype M12 (strain MGAS9429).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370551;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS9429;
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000259; ABF32738.1; -; Genomic_DNA.
DR RefSeq; WP_002988496.1; NC_008021.1.
DR AlphaFoldDB; Q1JK85; -.
DR SMR; Q1JK85; -.
DR EnsemblBacteria; ABF32738; ABF32738; MGAS9429_Spy1551.
DR GeneID; 57853232; -.
DR KEGG; spk:MGAS9429_Spy1551; -.
DR HOGENOM; CLU_074944_3_0_9; -.
DR OMA; LYRMRMY; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000002433; 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_1000010873"
SQ SEQUENCE 185 AA; 20467 MW; F90476AACDDE4DA5 CRC64;
MIEASKLKAG MTFEAEGKLI RVLEASHHKP GKGNTIMRMK LRDVRTGSTF DTTYRPDEKF
EQAIIETVPA QYLYKMDDTA YFMNTDTYDQ YEIPVANVEQ ELLYILENSD VKIQFYGSEV
IGVTVPTTVE LTVAETQPSI KGATVTGSGK PATLETGLVV NVPDFIEAGQ KLIINTAEGT
YVSRA