EFP_TREPS
ID EFP_TREPS Reviewed; 187 AA.
AC B2S3B8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-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=TPASS_0525;
OS Treponema pallidum subsp. pallidum (strain SS14).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=455434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS14;
RX PubMed=18482458; DOI=10.1186/1471-2180-8-76;
RA Matejkova P., Strouhal M., Smajs D., Norris S.J., Palzkill T.,
RA Petrosino J.F., Sodergren E., Norton J.E., Singh J., Richmond T.A.,
RA Molla M.N., Albert T.J., Weinstock G.M.;
RT "Complete genome sequence of Treponema pallidum ssp. pallidum strain SS14
RT determined with oligonucleotide arrays.";
RL BMC Microbiol. 8:76-76(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000805; ACD70947.1; -; Genomic_DNA.
DR RefSeq; WP_010881973.1; NC_021508.1.
DR AlphaFoldDB; B2S3B8; -.
DR SMR; B2S3B8; -.
DR EnsemblBacteria; ACD70947; ACD70947; TPASS_0525.
DR GeneID; 57879048; -.
DR KEGG; tpp:TPASS_0525; -.
DR PATRIC; fig|455434.6.peg.523; -.
DR OMA; WSVVEFQ; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000001202; 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..187
FT /note="Elongation factor P"
FT /id="PRO_1000096220"
SQ SEQUENCE 187 AA; 21043 MW; 49587D4560678ECA CRC64;
MIRGGDIAKG TVLLHKGAPY LVVEREFVNP GKGAAFARVK MKHLRDGSVL TQTVKTSDTV
EDAVVDSHRA QYQYDDGECF VFMDTRSFEQ IFVSKGNVPG RERYLREGDE YDILIWNGES
IDIKIPTKMV FRVAHSEPYL KGDTVSGATK PVTTETGLVV RVPLFIKQGE KILINTETNE
YQERVND
