ID A0A3N1ARX4_9ACTN Unreviewed; 185 AA.
AC A0A3N1ARX4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Elongation factor P {ECO:0000256|HAMAP-Rule:MF_00141};
DE Short=EF-P {ECO:0000256|HAMAP-Rule:MF_00141};
GN Name=efp {ECO:0000256|HAMAP-Rule:MF_00141};
GN ORFNames=EDC02_1336 {ECO:0000313|EMBL:ROO59536.1};
OS Micromonospora sp. Llam0.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2485143 {ECO:0000313|EMBL:ROO59536.1, ECO:0000313|Proteomes:UP000275308};
RN [1] {ECO:0000313|EMBL:ROO59536.1, ECO:0000313|Proteomes:UP000275308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Llam0 {ECO:0000313|EMBL:ROO59536.1,
RC ECO:0000313|Proteomes:UP000275308};
RA D'Agostino P.;
RT "Genome mining of underrepresented organisms for secondary metabolites.";
RL Submitted (NOV-2018) 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: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:ROO59536.1}.
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DR EMBL; RJJY01000001; ROO59536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1ARX4; -.
DR OrthoDB; 9801844at2; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000275308; 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:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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; 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}; Initiation factor {ECO:0000313|EMBL:ROO59536.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00141}; Reference proteome {ECO:0000313|Proteomes:UP000275308}.
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 185 AA; 19948 MW; E72332A6DC6CEAC5 CRC64;
MATTNDLKNG LVLNLDGELW AVVEFQHVKP GKGGAFVRTT LKNVLSGKVV DKTFNAGTKV
DTATVDKRTM QYLYADGEDY VFMDLETFDQ IMVPGGTVGE AANYLLPEAE AIVATHEGVP
LYVELPTSVV LEVTYTEPGL QGDRSTGGNK PATMETGATV QVPLFVTTGE KIKVDTRDGR
YLGRA
//
