ID   EFP_JANSC               Reviewed;         187 AA.
AC   Q28M91;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   02-MAR-2010, entry version 32.
DE   RecName: Full=Elongation factor P;
DE            Short=EF-P;
GN   Name=efp; OrderedLocusNames=Jann_3254;
OS   Jannaschia sp. (strain CCS1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Jannaschia.
OX   NCBI_TaxID=290400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E.,
RA   Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A.,
RA   Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT   "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in peptide bond synthesis. Stimulates efficient
CC       translation and peptide-bond synthesis on native or reconstituted
CC       70S ribosomes in vitro. Probably functions indirectly by altering
CC       the affinity of the ribosome for aminoacyl-tRNA, thus increasing
CC       their reactivity as acceptors for peptidyl transferase (By
CC       similarity).
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the elongation factor P family.
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DR   EMBL; CP000264; ABD56171.1; -; Genomic_DNA.
DR   RefSeq; YP_511196.1; -.
DR   SMR; Q28M91; 4-187.
DR   STRING; Q28M91; -.
DR   GeneID; 3935726; -.
DR   GenomeReviews; CP000264_GR; Jann_3254.
DR   KEGG; jan:Jann_3254; -.
DR   eggNOG; COG0231; -.
DR   HOGENOM; HBG303311; -.
DR   OMA; MISSNDF; -.
DR   PhylomeDB; Q28M91; -.
DR   ProtClustDB; PRK00529; -.
DR   BioCyc; JSP290400:JANN_3254-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:HAMAP.
DR   GO; GO:0006414; P:translational elongation; IEA:HAMAP.
DR   HAMAP; MF_00141; EF-P; 1; -.
DR   InterPro; IPR015365; Elong-fact-P_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
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; IPR014722; Transl_SH3-like_sub.
DR   InterPro; IPR008991; Translation_prot_SH3-like.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 2.
DR   Gene3D; G3DSA:2.30.30.30; Ribosomal_L2; 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; SM00841; Elong-fact-P_C; 1.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 2.
DR   SUPFAM; SSF50104; Transl_SH3_like; 1.
DR   TIGRFAMs; TIGR00038; efp; 1.
DR   PROSITE; PS01275; EFP; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Elongation factor; Protein biosynthesis.
FT   CHAIN         1    187       Elongation factor P.
FT                                /FTId=PRO_1000010764.
SQ   SEQUENCE   187 AA;  20896 MW;  87B3A4176AF2A2D0 CRC64;
     MPKINGNEIR PGNVLEHNGG LWAAVKVDHV KPGKGGAFAQ VELRNLRNGS KLNERFRSAD
     KVERVRLEQK DQQFLYESDG MLVFMDAETY EQIELPAELL GERRPFLQDG MTIVVEFHDD
     EALNASLPQK VVCKVVETEP VVKGQTAANS FKPAILDNGV KVMVPPFVGQ DEDIVVNTET
     MDYSERA
//