ID   EFP_SHEON               Reviewed;         186 AA.
AC   Q8EEP9;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=SO_2328;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
RN   [2]
RP   GLYCOSYLATION AT ARG-32, AND MUTAGENESIS OF ARG-32.
RX   PubMed=25686373; DOI=10.1038/nchembio.1751;
RA   Lassak J., Keilhauer E.C., Fuerst M., Wuichet K., Goedeke J.,
RA   Starosta A.L., Chen J.M., Soegaard-Andersen L., Rohr J., Wilson D.N.,
RA   Haeussler S., Mann M., Jung K.;
RT   "Arginine-rhamnosylation as new strategy to activate translation elongation
RT   factor P.";
RL   Nat. Chem. Biol. 11:266-270(2015).
RN   [3]
RP   GLYCOSYLATION AT ARG-32.
RX   PubMed=28451135; DOI=10.1039/c6sc02889f;
RA   Li X., Krafczyk R., Macosek J., Li Y.L., Zou Y., Simon B., Pan X., Wu Q.Y.,
RA   Yan F., Li S., Hennig J., Jung K., Lassak J., Hu H.G.;
RT   "Resolving the alpha-glycosidic linkage of arginine-rhamnosylated
RT   translation elongation factor P triggers generation of the first ArgRha
RT   specific antibody.";
RL   Chem. Sci. 7:6995-7001(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:25686373}.
CC   -!- SIMILARITY: Belongs to the elongation factor P family.
CC       {ECO:0000255|HAMAP-Rule:MF_00141}.
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; AE014299; AAN55362.1; -; Genomic_DNA.
DR   RefSeq; NP_717918.1; NC_004347.2.
DR   RefSeq; WP_011072320.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EEP9; -.
DR   SMR; Q8EEP9; -.
DR   STRING; 211586.SO_2328; -.
DR   PaxDb; Q8EEP9; -.
DR   KEGG; son:SO_2328; -.
DR   PATRIC; fig|211586.12.peg.2243; -.
DR   eggNOG; COG0231; Bacteria.
DR   HOGENOM; CLU_074944_2_1_6; -.
DR   OMA; WSVVEFQ; -.
DR   OrthoDB; 1260763at2; -.
DR   PhylomeDB; Q8EEP9; -.
DR   BioCyc; SONE211586:G1GMP-2127-MON; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
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;
KW   Reference proteome.
FT   CHAIN           1..186
FT                   /note="Elongation factor P"
FT                   /id="PRO_0000094325"
FT   CARBOHYD        32
FT                   /note="N-alpha-linked (Rha) arginine"
FT                   /evidence="ECO:0000269|PubMed:25686373,
FT                   ECO:0000269|PubMed:28451135"
FT   MUTAGEN         32
FT                   /note="R->A,K: Abolished arginine rhamnosylation."
FT                   /evidence="ECO:0000269|PubMed:25686373"
SQ   SEQUENCE   186 AA;  20619 MW;  C96110D65597507C CRC64;
     MKTAHEVRPG NVIMFEGSPW VVQKTETTRS GRNAAIVKLK LKNLLLNSGT ETTFKGEDKI
     DDIILDRLDC TYSYFADPMY VFMDAEYNQY DVEAENLGDA AAYIVDGMEE TCQVTFYDGK
     AISVEMPTTI VREVIYTEPS ARGDTSGKVM KPATITGGGT ISVADFVKVG DKIEIDTRTG
     EFKKRV