ID E3GFW4_9FIRM Unreviewed; 185 AA.
AC E3GFW4; A0A1M6VWP7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=Elongation factor P {ECO:0000256|HAMAP-Rule:MF_00141};
DE Short=EF-P {ECO:0000256|HAMAP-Rule:MF_00141};
GN Name=efp {ECO:0000256|HAMAP-Rule:MF_00141,
GN ECO:0000313|EMBL:NZA37711.1};
GN OrderedLocusNames=ELI_3489 {ECO:0000313|EMBL:ADO38448.1};
GN ORFNames=H0N91_06045 {ECO:0000313|EMBL:NZA37711.1},
GN SAMN04487888_105334 {ECO:0000313|EMBL:SFO88532.1};
OS Eubacterium callanderi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=53442 {ECO:0000313|EMBL:ADO38448.1, ECO:0000313|Proteomes:UP000006873};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KIST612;
RA Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H., Chang I.S.,
RA Choi I.-G.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO38448.1, ECO:0000313|Proteomes:UP000006873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIST612 {ECO:0000313|EMBL:ADO38448.1,
RC ECO:0000313|Proteomes:UP000006873};
RX PubMed=21036996; DOI=10.1128/JB.01217-10;
RA Roh H., Ko H.J., Kim D., Choi D.G., Park S., Kim S., Chang I.S., Choi I.G.;
RT "Complete genome sequence of a carbon monoxide-utilizing acetogen,
RT Eubacterium limosum KIST612.";
RL J. Bacteriol. 193:307-308(2011).
RN [3] {ECO:0000313|EMBL:SFO88532.1, ECO:0000313|Proteomes:UP000199443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NLAE-zl-G225 {ECO:0000313|EMBL:SFO88532.1,
RC ECO:0000313|Proteomes:UP000199443};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:NZA37711.1, ECO:0000313|Proteomes:UP000586254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMC0717 {ECO:0000313|EMBL:NZA37711.1,
RC ECO:0000313|Proteomes:UP000586254};
RA Marsh A.J., Azcarate-Peril M.A.;
RT "Organ Donor 1.";
RL Submitted (JUL-2020) 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.
CC {ECO:0000256|ARBA:ARBA00025469, ECO:0000256|HAMAP-Rule:MF_00141}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000256|ARBA:ARBA00004815, ECO:0000256|HAMAP-Rule:MF_00141}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00141}.
CC -!- SIMILARITY: Belongs to the elongation factor P family.
CC {ECO:0000256|ARBA:ARBA00009479, ECO:0000256|HAMAP-Rule:MF_00141,
CC ECO:0000256|RuleBase:RU004389}.
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DR EMBL; CP002273; ADO38448.1; -; Genomic_DNA.
DR EMBL; JACCKS010000005; NZA37711.1; -; Genomic_DNA.
DR EMBL; FOWI01000005; SFO88532.1; -; Genomic_DNA.
DR RefSeq; WP_013381755.1; NZ_QYRZ01000013.1.
DR AlphaFoldDB; E3GFW4; -.
DR GeneID; 68364431; -.
DR KEGG; elm:ELI_3489; -.
DR eggNOG; COG0231; Bacteria.
DR HOGENOM; CLU_074944_0_1_9; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000006873; Chromosome.
DR Proteomes; UP000199443; Unassembled WGS sequence.
DR Proteomes; UP000586254; Unassembled WGS sequence.
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; Nucleic acid-binding proteins; 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_uL2_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 NCBIfam; TIGR00038; efp; 1.
DR PANTHER; PTHR30053; ELONGATION FACTOR P; 1.
DR PANTHER; PTHR30053:SF12; ELONGATION FACTOR P (EF-P) FAMILY PROTEIN; 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; SSF50249; Nucleic acid-binding proteins; 2.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR PROSITE; PS01275; EFP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00141};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW Rule:MF_00141};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00141}.
FT DOMAIN 67..121
FT /note="Translation elongation factor P/YeiP central"
FT /evidence="ECO:0000259|SMART:SM01185"
FT DOMAIN 129..184
FT /note="Elongation factor P C-terminal"
FT /evidence="ECO:0000259|SMART:SM00841"
SQ SEQUENCE 185 AA; 20736 MW; B63175E5A0BFB1F7 CRC64;
MISAGEFKKG VTFEMDGSVF MIVEFQHVKP GKGAAFVRTK IRNVLTGAVV EKTFSPTEKF
PKAHIDTKEM QYLYADGDLY YFMDLETYEQ IPLNYDQVED ALKFLKENDN ATIRFFKGEA
FSVAAPNFVE LLITKTEPGF KGDTATGANK PATLETGAVI TVPLFVEEGD TIRVDTRTGE
YMERV
//
