EFP_THET8
ID EFP_THET8 Reviewed; 184 AA.
AC Q76G20; Q5SJ89;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Elongation factor P;
DE Short=EF-P;
GN Name=efp; OrderedLocusNames=TTHA1125;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (1.65
RP ANGSTROMS).
RX PubMed=15210970; DOI=10.1073/pnas.0308667101;
RA Hanawa-Suetsugu K., Sekine S., Sakai H., Hori-Takemoto C., Terada T.,
RA Unzai S., Tame J.R.H., Kuramitsu S., Shirouzu M., Yokoyama S.;
RT "Crystal structure of elongation factor P from Thermus thermophilus HB8.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9595-9600(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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 (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; AB103477; BAD14383.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70948.1; -; Genomic_DNA.
DR RefSeq; WP_011173195.1; NC_006461.1.
DR RefSeq; YP_144391.1; NC_006461.1.
DR PDB; 1UEB; X-ray; 1.65 A; A/B=1-184.
DR PDB; 4V6A; X-ray; 3.10 A; AV/CV=1-184.
DR PDBsum; 1UEB; -.
DR PDBsum; 4V6A; -.
DR AlphaFoldDB; Q76G20; -.
DR SMR; Q76G20; -.
DR IntAct; Q76G20; 50.
DR STRING; 300852.55772507; -.
DR EnsemblBacteria; BAD70948; BAD70948; BAD70948.
DR GeneID; 3169027; -.
DR KEGG; ttj:TTHA1125; -.
DR PATRIC; fig|300852.9.peg.1104; -.
DR eggNOG; COG0231; Bacteria.
DR HOGENOM; CLU_074944_0_1_0; -.
DR OMA; WSVVEFQ; -.
DR PhylomeDB; Q76G20; -.
DR UniPathway; UPA00345; -.
DR EvolutionaryTrace; Q76G20; -.
DR Proteomes; UP000000532; 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..184
FT /note="Elongation factor P"
FT /id="PRO_0000094357"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 18..30
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 36..47
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 65..76
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1UEB"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:1UEB"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1UEB"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:1UEB"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:1UEB"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:1UEB"
SQ SEQUENCE 184 AA; 20225 MW; 962699782753CB30 CRC64;
MISVTDLRPG TKVKMDGGLW ECVEYQHQKL GRGGAKVVAK FKNLETGATV ERTFNSGEKL
EDIYVETREL QYLYPEGEEM VFMDLETYEQ FAVPRSRVVG AEFFKEGMTA LGDMYEGQPI
KVTPPTVVEL KVVDTPPGVR GDTVSGGSKP ATLETGAVVQ VPLFVEPGEV IKVDTRTGEY
VGRA
