(data stored in ACNUC7421 zone)

SWISSPROT: EFP_PSEHT

ID   EFP_PSEHT               Reviewed;         188 AA.
AC   Q3IFP5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 81.
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};
GN   OrderedLocusNames=PSHAa0474;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Involved in peptide bond synthesis. Alleviates ribosome
CC       stalling that occurs when 3 or more consecutive Pro residues or
CC       the sequence PPG is present in a protein, possibly by augmenting
CC       the peptidyl transferase activity of the ribosome. Modification of
CC       Lys-34 is required for alleviation. {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: May be beta-lysylated on the epsilon-amino group of Lys-34 by
CC       the combined action of EpmA and EpmB, and then hydroxylated on the
CC       C5 position of the same residue by EpmC (if this protein is
CC       present). Lysylation is critical for the stimulatory effect of EF-
CC       P on peptide-bond formation. The lysylation moiety may extend
CC       toward the peptidyltransferase center and stabilize the terminal
CC       3-CCA end of the tRNA. Hydroxylation of the C5 position on Lys-34
CC       may allow additional potential stabilizing hydrogen-bond
CC       interactions with the P-tRNA. {ECO:0000255|HAMAP-Rule:MF_00141}.
CC   -!- SIMILARITY: Belongs to the elongation factor P family.
CC       {ECO:0000255|HAMAP-Rule:MF_00141}.
DR   EMBL; CR954246; CAI85571.1; -; Genomic_DNA.
DR   RefSeq; WP_011327184.1; NC_007481.1.
DR   ProteinModelPortal; Q3IFP5; -.
DR   SMR; Q3IFP5; -.
DR   STRING; 326442.PSHAa0474; -.
DR   EnsemblBacteria; CAI85571; CAI85571; PSHAa0474.
DR   GeneID; 32566660; -.
DR   KEGG; pha:PSHAa0474; -.
DR   PATRIC; fig|326442.8.peg.451; -.
DR   eggNOG; ENOG4105DRH; Bacteria.
DR   eggNOG; COG0231; LUCA.
DR   HOGENOM; HOG000010047; -.
DR   KO; K02356; -.
DR   OMA; NTFSAGH; -.
DR   OrthoDB; POG091H028W; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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   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.
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;
DR   PRODOM; Q3IFP5.
DR   SWISS-2DPAGE; Q3IFP5.
KW   Complete proteome; Cytoplasm; Elongation factor; Hydroxylation;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN         1    188       Elongation factor P.
FT                                /FTId=PRO_1000010815.
FT   MOD_RES      34     34       N6-(3,6-diaminohexanoyl)-5-hydroxylysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00141}.
SQ   SEQUENCE   188 AA;  20566 MW;  60DB35418266C780 CRC64;
     MANYSTNEFK GGLKIMMDGE PSSIIENEMV KPGKGQAFNR VRIRKLISGK VLEKTFKSGE
     SVEGADVMDT DLAYLYTDGE FWHFMNNETF EQIAADEKAL GDAGKWLVEN DVCTITLWNG
     NPIVVTPPNF VELEITETDP GLKGDTAGTG GKPATLSTGA VVRVPLFVQI GEVIKVDTRN
     GEYVSRVK
//

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