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Database: UniProt
Entry: I9H292_9BACE
LinkDB: I9H292_9BACE
Original site: I9H292_9BACE 
ID   I9H292_9BACE            Unreviewed;       188 AA.
AC   I9H292;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
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   ORFNames=HMPREF1068_00744 {ECO:0000313|EMBL:EIY53574.1};
OS   Bacteroides nordii CL02T12C05.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=997884 {ECO:0000313|EMBL:EIY53574.1, ECO:0000313|Proteomes:UP000003089};
RN   [1] {ECO:0000313|EMBL:EIY53574.1, ECO:0000313|Proteomes:UP000003089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL02T12C05 {ECO:0000313|EMBL:EIY53574.1,
RC   ECO:0000313|Proteomes:UP000003089};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA   Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Bacteroides nordii CL02T12C05.";
RL   Submitted (FEB-2012) 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:0000256|HAMAP-
CC       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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIY53574.1}.
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DR   EMBL; AGXS01000011; EIY53574.1; -; Genomic_DNA.
DR   RefSeq; WP_002558969.1; NZ_JH724314.1.
DR   AlphaFoldDB; I9H292; -.
DR   STRING; 997884.HMPREF1068_00744; -.
DR   GeneID; 77204526; -.
DR   PATRIC; fig|997884.3.peg.750; -.
DR   eggNOG; COG0231; Bacteria.
DR   HOGENOM; CLU_074944_0_1_10; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000003089; 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}; Reference proteome {ECO:0000313|Proteomes:UP000003089}.
FT   DOMAIN          67..122
FT                   /note="Translation elongation factor P/YeiP central"
FT                   /evidence="ECO:0000259|SMART:SM01185"
FT   DOMAIN          130..185
FT                   /note="Elongation factor P C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00841"
SQ   SEQUENCE   188 AA;  21254 MW;  A94659C67155F7D7 CRC64;
     MINAQDIKNG TCIRMDGKLY FCIEFLHVKP GKGNTFMRTK LKDVVSGYVL ERRFNIGEKL
     EDVRVERRPY QFLYKEGEDY IFMNQETFDQ HPIAHDLING VDFLLEGAVL DVVSDASTET
     VLYADMPIKV QMKVTYTEPG MKGDTATNTL KPATVESGAT VRVPLFINEG ETIEIDTRDG
     SYVGRVKA
//
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