ID A0A1F9D730_9DELT Unreviewed; 187 AA.
AC A0A1F9D730;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-NOV-2024, entry version 22.
DE RecName: Full=Elongation factor P {ECO:0000256|HAMAP-Rule:MF_00141, ECO:0000256|NCBIfam:TIGR00038};
DE Short=EF-P {ECO:0000256|HAMAP-Rule:MF_00141};
GN Name=efp {ECO:0000256|HAMAP-Rule:MF_00141};
GN ORFNames=A2031_02070 {ECO:0000313|EMBL:OGP90637.1};
OS Deltaproteobacteria bacterium RBG_19FT_COMBO_43_11.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1797849 {ECO:0000313|EMBL:OGP90637.1, ECO:0000313|Proteomes:UP000179178};
RN [1] {ECO:0000313|EMBL:OGP90637.1, ECO:0000313|Proteomes:UP000179178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:0000256|HAMAP-
CC Rule:MF_00141}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000256|ARBA:ARBA00004815, ECO:0000256|HAMAP-Rule:MF_00141}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00141}.
CC -!- SIMILARITY: Belongs to the elongation factor P family.
CC {ECO:0000256|ARBA:ARBA00009479, ECO:0000256|HAMAP-Rule:MF_00141,
CC ECO:0000256|RuleBase:RU004389}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGP90637.1}.
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DR EMBL; MGQZ01000030; OGP90637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F9D730; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000179178; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043043; P:peptide biosynthetic process; IEA:InterPro.
DR CDD; cd04470; S1_EF-P_repeat_1; 1.
DR CDD; cd05794; S1_EF-P_repeat_2; 1.
DR FunFam; 2.30.30.30:FF:000003; Elongation factor P; 1.
DR FunFam; 2.40.50.140:FF:000004; Elongation factor P; 1.
DR FunFam; 2.40.50.140:FF:000009; Elongation factor P; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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_uL2_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 NCBIfam; TIGR00038; efp; 1.
DR PANTHER; PTHR30053; ELONGATION FACTOR P; 1.
DR PANTHER; PTHR30053:SF12; ELONGATION FACTOR P (EF-P) FAMILY PROTEIN; 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; SSF50249; Nucleic acid-binding proteins; 2.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR PROSITE; PS01275; EFP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00141};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW Rule:MF_00141};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00141}.
FT DOMAIN 67..121
FT /note="Translation elongation factor P/YeiP central"
FT /evidence="ECO:0000259|SMART:SM01185"
FT DOMAIN 129..184
FT /note="Elongation factor P C-terminal"
FT /evidence="ECO:0000259|SMART:SM00841"
SQ SEQUENCE 187 AA; 21519 MW; 272AB1CBAA25D73D CRC64;
MYTASDLRKG LRLKIDNEPY VITEFNFVKP GKGQALYRTK LKNMITGSQF ERSFRSVDTF
EQADLREKKM QYLYKEGDKF CFMDNENYEQ VYLTQNQVGD AQNFLIDNLD VEILLFEDRP
IGLSLPNFVE LVVTEAEPWA KGDTVSGATK PVKLQTGYTI LVPTFVTEGE KIRVDTRTGE
YLTRVKG
//