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EFP_BRUA2
ID   EFP_BRUA2               Reviewed;         186 AA.
AC   Q2YRC4; Q57BH0; Q6XUV8;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=BAB1_1722;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Iannino F., Inon de Iannino N.;
RT   "Cloning and characterization of the Agrobacterium tumefaciens chvH homolog
RT   gene in Brucella abortus.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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   -!- SIMILARITY: Belongs to the elongation factor P family.
CC       {ECO:0000255|HAMAP-Rule:MF_00141}.
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DR   EMBL; AY208889; AAO48984.1; -; Genomic_DNA.
DR   EMBL; AM040264; CAJ11678.1; -; Genomic_DNA.
DR   RefSeq; WP_002964799.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YRC4; -.
DR   SMR; Q2YRC4; -.
DR   STRING; 359391.BAB1_1722; -.
DR   EnsemblBacteria; CAJ11678; CAJ11678; BAB1_1722.
DR   GeneID; 3788239; -.
DR   KEGG; bmf:BAB1_1722; -.
DR   PATRIC; fig|359391.11.peg.236; -.
DR   HOGENOM; CLU_074944_1_1_5; -.
DR   OMA; WSVVEFQ; -.
DR   PhylomeDB; Q2YRC4; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000002719; Chromosome I.
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; 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; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..186
FT                   /note="Elongation factor P"
FT                   /id="PRO_0000094212"
SQ   SEQUENCE   186 AA;  20700 MW;  0DB78F78885EC53A CRC64;
     MKINGNEIRP GNVIEHEGGL WVAVKTNAVK PGKGGAYNQV ELKNLINGTK LNERFRAAES
     VERVRLEQKD FSFLYEQGEA LIFMDTETYE QLELQKDFVG DRAAFLQDGM MVTVELYEEK
     PIGIRLPDQV TLAITEADPV VKGQTAASSY KPAVLENGIR IPVPPFIASG ERVIVDTNEL
     TYISRA
 
 
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