ID A0A0A1VDY7_9BURK Unreviewed; 184 AA.
AC A0A0A1VDY7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=AVS7_01247 {ECO:0000313|EMBL:GAD21487.1};
OS Acidovorax sp. MR-S7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1268622 {ECO:0000313|EMBL:GAD21487.1};
RN [1] {ECO:0000313|EMBL:GAD21487.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-S7 {ECO:0000313|EMBL:GAD21487.1};
RX DOI=10.1128/genomeA.00412-13;
RA Miura T., Kusada H., Kamagata Y., Hanada S., Kimura N.;
RT "Genome Sequence of the Multiple-beta-Lactam-Antibiotic-Resistant Bacterium
RT Acidovorax sp. Strain MR-S7.";
RL Genome Announc. 1:e00412-13(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DF238908; GAD21487.1; -; Genomic_DNA.
DR RefSeq; WP_020227537.1; NZ_DF238908.1.
DR AlphaFoldDB; A0A0A1VDY7; -.
DR STRING; 1268622.AVS7_01247; -.
DR eggNOG; COG0231; Bacteria.
DR OrthoDB; 9801844at2; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000030646; 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 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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00141}; Reference proteome {ECO:0000313|Proteomes:UP000030646}.
FT DOMAIN 67..120
FT /note="Translation elongation factor P/YeiP central"
FT /evidence="ECO:0000259|SMART:SM01185"
FT DOMAIN 128..183
FT /note="Elongation factor P C-terminal"
FT /evidence="ECO:0000259|SMART:SM00841"
SQ SEQUENCE 184 AA; 20498 MW; DE341584D4BD199B CRC64;
MKIAQEIRAG NVIMQGKDPM IVLKTEYARG GRGAATVRMK LKALLSNMGT EVVFKADDKI
DNVILDKKEC TYSYFADPMY VWMDTEYNQY EVEAGNMGDA ISYLEDGMSA EVVFYDGKAI
SVELPTSVER EITWTEPAVK GDTSGKVLKP AKIATGFEVA VPLFVDQGDK IEIDTRTGEY
RKRV
//
