ID   EFP_XANCP               Reviewed;         188 AA.
AC   Q8P8G9;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 108.
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=XCC2272;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: Involved in peptide bond synthesis. Alleviates ribosome
CC       stalling that occurs when 3 or more consecutive Pro residues or the
CC       sequence PPG is present in a protein, possibly by augmenting the
CC       peptidyl transferase activity of the ribosome. Modification of Lys-34
CC       is required for alleviation. {ECO:0000255|HAMAP-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: May be beta-lysylated on the epsilon-amino group of Lys-34 by the
CC       combined action of EpmA and EpmB, and then hydroxylated on the C5
CC       position of the same residue by EpmC (if this protein is present).
CC       Lysylation is critical for the stimulatory effect of EF-P on peptide-
CC       bond formation. The lysylation moiety may extend toward the
CC       peptidyltransferase center and stabilize the terminal 3-CCA end of the
CC       tRNA. Hydroxylation of the C5 position on Lys-34 may allow additional
CC       potential stabilizing hydrogen-bond interactions with the P-tRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_00141}.
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; AE008922; AAM41551.1; -; Genomic_DNA.
DR   RefSeq; NP_637627.1; NC_003902.1.
DR   RefSeq; WP_011037416.1; NC_003902.1.
DR   AlphaFoldDB; Q8P8G9; -.
DR   SMR; Q8P8G9; -.
DR   STRING; 340.xcc-b100_1906; -.
DR   EnsemblBacteria; AAM41551; AAM41551; XCC2272.
DR   GeneID; 58013151; -.
DR   KEGG; xcc:XCC2272; -.
DR   PATRIC; fig|190485.4.peg.2422; -.
DR   eggNOG; COG0231; Bacteria.
DR   HOGENOM; CLU_074944_0_0_6; -.
DR   OMA; WSVVEFQ; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000001010; 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; 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; Hydroxylation; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..188
FT                   /note="Elongation factor P"
FT                   /id="PRO_0000094373"
FT   MOD_RES         34
FT                   /note="N6-(3,6-diaminohexanoyl)-5-hydroxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00141"
SQ   SEQUENCE   188 AA;  20834 MW;  22B92B717980A938 CRC64;
     MATVGMNDVK NGMKILVNNE PAVITETEYV KPGKGQAFTR MKYRFIKSGR VVEMTMKATD
     DVEVADVVDT DMRYLYTDGE YWHFMDPESF EQVQADKAGM GGAEKWLKGE EDCIVTLWNG
     APIWVQPPNF VELKITETDP GVRGDTSGGG GKPATLETGA VVRVPLFVNQ DEVIKVDTRS
     GEYSARVK