ID   EFP2_GEOSL              Reviewed;         187 AA.
AC   Q74CC2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Elongation factor P 2 {ECO:0000255|HAMAP-Rule:MF_00141};
DE            Short=EF-P 2 {ECO:0000255|HAMAP-Rule:MF_00141};
GN   Name=efp2 {ECO:0000255|HAMAP-Rule:MF_00141}; Synonyms=efp-2;
GN   OrderedLocusNames=GSU1752;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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; AE017180; AAR35129.1; -; Genomic_DNA.
DR   RefSeq; NP_952802.1; NC_002939.5.
DR   RefSeq; WP_010942396.1; NC_002939.5.
DR   AlphaFoldDB; Q74CC2; -.
DR   SMR; Q74CC2; -.
DR   STRING; 243231.GSU1752; -.
DR   EnsemblBacteria; AAR35129; AAR35129; GSU1752.
DR   KEGG; gsu:GSU1752; -.
DR   PATRIC; fig|243231.5.peg.1792; -.
DR   eggNOG; COG0231; Bacteria.
DR   HOGENOM; CLU_074944_0_0_7; -.
DR   InParanoid; Q74CC2; -.
DR   OMA; WSVVEFQ; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
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..187
FT                   /note="Elongation factor P 2"
FT                   /id="PRO_0000094254"
SQ   SEQUENCE   187 AA;  21239 MW;  F5EB788BC36AA23A CRC64;
     MYTVADLKKG LKLTLDGAPY LVIAFEFSKP GKGQALYRTK MRNMITGVIL DRTYRSGETF
     EPARLEERRM QYLYKEDTHY TFMDNQTFEQ VQMDEDAVGD AKNFLIDNLE VDILLFGEKA
     IGVTLPNFVN LRVVQTDPWV KGDTSGSDSK PATVETGYIL RVPPFIEEGE MIVIDTRSGE
     YSTRVKG