EFP_STRP6
ID EFP_STRP6 Reviewed; 185 AA.
AC Q5XA92; P82459;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Elongation factor P;
DE Short=EF-P;
GN Name=efp; OrderedLocusNames=M6_Spy1536;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
RN [2]
RP PROTEIN SEQUENCE OF 1-11; 22-75 AND 142-185.
RC STRAIN=JRS4 / Serotype M6;
RA Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA VanBogelen R.A.;
RT "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT proteins.";
RL Submitted (APR-2000) to UniProtKB.
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; CP000003; AAT87671.1; -; Genomic_DNA.
DR RefSeq; WP_002988496.1; NC_006086.1.
DR AlphaFoldDB; Q5XA92; -.
DR SMR; Q5XA92; -.
DR EnsemblBacteria; AAT87671; AAT87671; M6_Spy1536.
DR GeneID; 57853232; -.
DR KEGG; spa:M6_Spy1536; -.
DR HOGENOM; CLU_074944_3_0_9; -.
DR OMA; LYRMRMY; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000001167; 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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor;
KW Protein biosynthesis.
FT CHAIN 1..185
FT /note="Elongation factor P"
FT /id="PRO_0000094345"
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
