EFP_BACFR
ID EFP_BACFR Reviewed; 188 AA.
AC P70889; Q64Z41;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Elongation factor P;
DE Short=EF-P;
GN Name=efp; OrderedLocusNames=BF0486;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BF1;
RX PubMed=9648740; DOI=10.1007/s004380050742;
RA Abratt V.R., Mbewe M., Woods D.R.;
RT "Cloning of an EF-P homologue from Bacteroides fragilis that increases B.
RT fragilis glutamine synthetase activity in Escherichia coli.";
RL Mol. Gen. Genet. 258:363-372(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; U75509; AAC26328.1; -; Genomic_DNA.
DR EMBL; AP006841; BAD47235.1; -; Genomic_DNA.
DR RefSeq; WP_005784338.1; NZ_UYXF01000019.1.
DR RefSeq; YP_097769.1; NC_006347.1.
DR AlphaFoldDB; P70889; -.
DR SMR; P70889; -.
DR STRING; 295405.BF0486; -.
DR EnsemblBacteria; BAD47235; BAD47235; BF0486.
DR GeneID; 66330465; -.
DR KEGG; bfr:BF0486; -.
DR PATRIC; fig|295405.11.peg.502; -.
DR HOGENOM; CLU_074944_0_1_10; -.
DR OMA; WSVVEFQ; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000002197; 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..188
FT /note="Elongation factor P"
FT /id="PRO_0000094195"
FT CONFLICT 20..22
FT /note="Missing (in Ref. 1; AAC26328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 21225 MW; 14374B7C0C92F9A6 CRC64;
MINAQDIKNG TCIRMDGKLY FCIEFLHVKP GKGNTFMRTK LKDVVSGYVL ERRFNIGEKL
EDVRVERRPY QYLYKEGEDY IFMNQETFDQ HPIAHDLING VDFLLEGAVV EVVSDASTET
VLYADMPIKV QMKVTYTEPG LKGDTATNTL KPATVESGAT VRVPLFISEG ETIEIDTRDG
SYVGRVKA