EFP_METC4
ID EFP_METC4 Reviewed; 188 AA.
AC B7KT38;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Mchl_3230;
OS Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=440085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM4 / NCIMB 13688;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT CM4.";
RL Submitted (DEC-2008) 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 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; CP001298; ACK84068.1; -; Genomic_DNA.
DR RefSeq; WP_003599274.1; NC_011757.1.
DR AlphaFoldDB; B7KT38; -.
DR SMR; B7KT38; -.
DR EnsemblBacteria; ACK84068; ACK84068; Mchl_3230.
DR KEGG; mch:Mchl_3230; -.
DR HOGENOM; CLU_074944_1_1_5; -.
DR OMA; RWRTTEQ; -.
DR BioCyc; MEXT440085:MCHL_RS15735-MON; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000002385; Chromosome.
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.
FT CHAIN 1..188
FT /note="Elongation factor P"
FT /id="PRO_1000123016"
SQ SEQUENCE 188 AA; 20743 MW; 4163B6D09BD2E365 CRC64;
MKVIASTLRK GNVVDKDGKL YVILTAENIH PGKGTPVTQL DMRRITDGVK ISERYRTTEQ
VERAFVEDRD HTFLYQDGEG YHFMNPESYE QIAVPADVVG DAAPYLQEGM TVTLSTHNGV
PLTIELPQRM TFEIVETEPV TKGQTASSSY KPALLSNGVK TSVPPHVSTG TRVVIMTADG
SYVERAKD
