ID   EFP_PSEPK               Reviewed;         189 AA.
AC   Q88LS0;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=PP_1858;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
RN   [2]
RP   GLYCOSYLATION AT ARG-32.
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=28951478; DOI=10.1128/mbio.01412-17;
RA   Krafczyk R., Macosek J., Jagtap P.K.A., Gast D., Wunder S., Mitra P.,
RA   Jha A.K., Rohr J., Hoffmann-Roder A., Jung K., Hennig J., Lassak J.;
RT   "Structural basis for EarP-mediated arginine glycosylation of translation
RT   elongation factor EF-P.";
RL   MBio 8:0-0(2017).
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:0000250|UniProtKB:Q9HZZ2}.
CC   -!- SIMILARITY: Belongs to the elongation factor P family.
CC       {ECO:0000255|HAMAP-Rule:MF_00141}.
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DR   EMBL; AE015451; AAN67477.1; -; Genomic_DNA.
DR   RefSeq; NP_744013.1; NC_002947.4.
DR   RefSeq; WP_003252871.1; NC_002947.4.
DR   AlphaFoldDB; Q88LS0; -.
DR   SMR; Q88LS0; -.
DR   STRING; 160488.PP_1858; -.
DR   EnsemblBacteria; AAN67477; AAN67477; PP_1858.
DR   KEGG; ppu:PP_1858; -.
DR   PATRIC; fig|160488.4.peg.1959; -.
DR   eggNOG; COG0231; Bacteria.
DR   HOGENOM; CLU_074944_2_1_6; -.
DR   OMA; RWRTTEQ; -.
DR   PhylomeDB; Q88LS0; -.
DR   BioCyc; PPUT160488:G1G01-1962-MON; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000000556; 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; 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..189
FT                   /note="Elongation factor P"
FT                   /id="PRO_0000094311"
FT   CARBOHYD        32
FT                   /note="N-alpha-linked (Rha) arginine"
FT                   /evidence="ECO:0000269|PubMed:28951478"
SQ   SEQUENCE   189 AA;  21303 MW;  F24A86314A354824 CRC64;
     MKTGKELKPG TVLRIDNDPW LVQKAEFTKS GRNSAIMKTK LKNLLTGYKT ETVYGADDKL
     DDVILDRKEA TLSFINGDEY TFMDTTDYTM YELNAEDIEA VLPYIEEGME DVCEAVFFEG
     RLVSVELPTT ISRKVVYTEN AARGDTSGKV MKPAKLANGT EISVADFIQI DEWIDIDTRD
     NSFKGRSKK