EFP_NEIME
ID EFP_NEIME Reviewed; 186 AA.
AC P0DUK0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 25-MAY-2022, entry version 4.
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};
OS Neisseria meningitidis.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=487;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, GLYCOSYLATION AT
RP ARG-32, AND MUTAGENESIS OF ARG-32.
RC STRAIN=NIID280;
RX PubMed=26840407; DOI=10.1371/journal.pone.0147907;
RA Yanagisawa T., Takahashi H., Suzuki T., Masuda A., Dohmae N., Yokoyama S.;
RT "Neisseria meningitidis translation elongation factor P and its active-site
RT arginine residue are essential for cell viability.";
RL PLoS ONE 11:e0147907-e0147907(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: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 -!- PTM: Glycosylated ar Arg-32 by EarP: arginine rhamnosylation is
CC required for EF-P function and rescue of polyproline stalled ribosomes.
CC {ECO:0000269|PubMed:26840407}.
CC -!- DISRUPTION PHENOTYPE: Lethality. {ECO:0000269|PubMed:26840407}.
CC -!- SIMILARITY: Belongs to the elongation factor P family.
CC {ECO:0000255|HAMAP-Rule:MF_00141}.
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DR EMBL; LC059994; BAU19338.1; -; Genomic_DNA.
DR RefSeq; WP_002213793.1; NZ_WSPC01000005.1.
DR AlphaFoldDB; P0DUK0; -.
DR SMR; P0DUK0; -.
DR OMA; LYRMRMY; -.
DR UniPathway; UPA00345; -.
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; 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.
PE 1: Evidence at protein level;
KW Cytoplasm; Elongation factor; Glycoprotein; Protein biosynthesis.
FT CHAIN 1..186
FT /note="Elongation factor P"
FT /id="PRO_0000452684"
FT CARBOHYD 32
FT /note="N-alpha-linked (Rha) arginine"
FT /evidence="ECO:0000269|PubMed:26840407"
FT MUTAGEN 32
FT /note="R->A,K: Induces lethality when transfected in cells
FT with deletion of efp gene."
FT /evidence="ECO:0000269|PubMed:26840407"
SQ SEQUENCE 186 AA; 20894 MW; 3502433BE9C04289 CRC64;
MKTAQELRAG NVFMVGNDPM VVQKTEYIKG GRSSAKVSMK LKNLLTGAAS ETIYKADDKF
DVVILSRKNC TYSYFADPMY VFMDEEFNQY EIEADNIGDA LKFIVDGMED QCEVTFYEGN
PISVELPTII VREVEYTEPA VKGDTSGKVM KTARLVGGTE IQVMSYIENG DKIEIDTRTG
EFRKRA
