EFP_ACET2
ID EFP_ACET2 Reviewed; 185 AA.
AC A3DDQ3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Cthe_0847;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000568; ABN52082.1; -; Genomic_DNA.
DR RefSeq; WP_003517139.1; NC_009012.1.
DR PDB; 1YBY; X-ray; 1.95 A; A/B=1-185.
DR PDBsum; 1YBY; -.
DR AlphaFoldDB; A3DDQ3; -.
DR SMR; A3DDQ3; -.
DR STRING; 203119.Cthe_0847; -.
DR EnsemblBacteria; ABN52082; ABN52082; Cthe_0847.
DR KEGG; cth:Cthe_0847; -.
DR eggNOG; COG0231; Bacteria.
DR HOGENOM; CLU_074944_0_1_9; -.
DR OMA; WSVVEFQ; -.
DR OrthoDB; 1260763at2; -.
DR UniPathway; UPA00345; -.
DR EvolutionaryTrace; A3DDQ3; -.
DR Proteomes; UP000002145; 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 3D-structure; Cytoplasm; Elongation factor; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..185
FT /note="Elongation factor P"
FT /id="PRO_1000010724"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:1YBY"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1YBY"
FT STRAND 18..28
FT /evidence="ECO:0007829|PDB:1YBY"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:1YBY"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1YBY"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1YBY"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:1YBY"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1YBY"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1YBY"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:1YBY"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:1YBY"
FT TURN 99..104
FT /evidence="ECO:0007829|PDB:1YBY"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:1YBY"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:1YBY"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:1YBY"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:1YBY"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:1YBY"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1YBY"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:1YBY"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1YBY"
SQ SEQUENCE 185 AA; 20654 MW; 0B9E5532C74794FE CRC64;
MISAGDFKNG VTFELDGQIF QVIEFQHVKP GKGAAFVRTK LKNIVTGATI EKTFNPTDKM
PKAHIERKDM QYLYNDGDLY YFMDTETFEQ LPLGKDKIGD ALKFVKENEI VKVLSHKGNV
FGIEPPNFVE LEVTDTEPGF KGDTATGATK PAIVETGASI KVPLFVNKGD IIRIDTRTGE
YMERV
