EFP_NITEC
ID EFP_NITEC Reviewed; 185 AA.
AC Q0AGI0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
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}; OrderedLocusNames=Neut_1302;
OS Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=335283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101675 / C91 / Nm57;
RX PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.;
RT "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas
RT eutropha C91: implications for niche adaptation.";
RL Environ. Microbiol. 9:2993-3007(2007).
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 -!- SIMILARITY: Belongs to the elongation factor P family.
CC {ECO:0000255|HAMAP-Rule:MF_00141}.
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DR EMBL; CP000450; ABI59552.1; -; Genomic_DNA.
DR RefSeq; WP_011634371.1; NC_008344.1.
DR AlphaFoldDB; Q0AGI0; -.
DR SMR; Q0AGI0; -.
DR STRING; 335283.Neut_1302; -.
DR EnsemblBacteria; ABI59552; ABI59552; Neut_1302.
DR KEGG; net:Neut_1302; -.
DR eggNOG; COG0231; Bacteria.
DR HOGENOM; CLU_074944_2_1_4; -.
DR OMA; WSVVEFQ; -.
DR OrthoDB; 1260763at2; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000001966; 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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; Protein biosynthesis.
FT CHAIN 1..185
FT /note="Elongation factor P"
FT /id="PRO_1000010791"
SQ SEQUENCE 185 AA; 21142 MW; 225DD9E229496435 CRC64;
MKTAQELRVG NVFMLGRDPM VVLKTEFTKS GRNSSVVKMK YKNLLTESPG EAVYKADDKF
DIVVLEKKEV SYSYYASPMY VFMDAEFNQY EVEEETMSDV LSFLEDGMPC EVVFYNDKPI
SVEMPNSVVR EIIYTEPAVK GDTSGKVMKS AKIVTGFELP VPLFCEIGDK IEIDTRTREY
RSRVK
