(data stored in SCRATCH zone)

SWISSPROT: C5BDL2_EDWI9

ID   C5BDL2_EDWI9            Unreviewed;       188 AA.
AC   C5BDL2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 2.
DT   07-JUN-2017, entry version 61.
DE   RecName: Full=Elongation factor P {ECO:0000256|HAMAP-Rule:MF_00141};
DE            Short=EF-P {ECO:0000256|HAMAP-Rule:MF_00141};
GN   Name=efp {ECO:0000256|HAMAP-Rule:MF_00141};
GN   OrderedLocusNames=NT01EI_0387 {ECO:0000313|EMBL:ACR67628.2};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67628.2, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC       Rule:MF_00141}.
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC       {ECO:0000256|HAMAP-Rule:MF_00141}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00141}.
CC   -!- SIMILARITY: Belongs to the elongation factor P family.
CC       {ECO:0000256|HAMAP-Rule:MF_00141, ECO:0000256|RuleBase:RU004389}.
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DR   EMBL; CP001600; ACR67628.2; -; Genomic_DNA.
DR   RefSeq; WP_015869834.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0387; -.
DR   EnsemblBacteria; ACR67628; ACR67628; NT01EI_0387.
DR   GeneID; 7960167; -.
DR   KEGG; eic:NT01EI_0387; -.
DR   PATRIC; fig|634503.3.peg.351; -.
DR   eggNOG; ENOG4105DRH; Bacteria.
DR   eggNOG; COG0231; LUCA.
DR   HOGENOM; HOG000010047; -.
DR   KO; K02356; -.
DR   OrthoDB; POG091H028W; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP.
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; C5BDL2.
DR   SWISS-2DPAGE; C5BDL2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00141};
KW   Elongation factor {ECO:0000256|HAMAP-Rule:MF_00141,
KW   ECO:0000313|EMBL:ACR67628.2};
KW   Hydroxylation {ECO:0000256|HAMAP-Rule:MF_00141};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN       69    123       EFP. {ECO:0000259|SMART:SM01185}.
FT   DOMAIN      131    186       Elong-fact-P_C. {ECO:0000259|SMART:
FT                                SM00841}.
FT   MOD_RES      34     34       N6-(3,6-diaminohexanoyl)-5-hydroxylysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00141}.
SQ   SEQUENCE   188 AA;  20517 MW;  50DCEA9EDBAD7755 CRC64;
     MATYSSNDFR SGLKIMMDGE PYAVESSEFV KPGKGQAFAR VKLRRLLTGK LIEKTFKSTD
     SAEGADVMDV NLTYLYNDGE FWHFMNNDTF EQLAADAKAV GDNAKWLLDQ AECVVTLWNG
     QPIAVTPPNF VELEIVETDP GLKGDTAGTG GKPATLTTGA VVKVPLFVQI GEVIKVDTRS
     GEYVSRVK
//

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