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Database: UniProt
Entry: U2UXK6_9FIRM
LinkDB: U2UXK6_9FIRM
Original site: U2UXK6_9FIRM 
ID   U2UXK6_9FIRM            Unreviewed;       195 AA.
AC   U2UXK6;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=HMPREF1985_00924 {ECO:0000313|EMBL:ERL05171.1};
OS   Mitsuokella sp. oral taxon 131 str. W9106.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Mitsuokella.
OX   NCBI_TaxID=1321781 {ECO:0000313|EMBL:ERL05171.1, ECO:0000313|Proteomes:UP000016614};
RN   [1] {ECO:0000313|EMBL:ERL05171.1, ECO:0000313|Proteomes:UP000016614}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W9106 {ECO:0000313|EMBL:ERL05171.1,
RC   ECO:0000313|Proteomes:UP000016614};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) 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}.
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:ERL05171.1}.
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DR   EMBL; AWVT01000009; ERL05171.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2UXK6; -.
DR   STRING; 1321781.HMPREF1985_00924; -.
DR   PATRIC; fig|1321781.3.peg.880; -.
DR   eggNOG; COG0231; Bacteria.
DR   HOGENOM; CLU_074944_0_1_9; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000016614; 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:UP000016614}.
FT   DOMAIN          77..131
FT                   /note="Translation elongation factor P/YeiP central"
FT                   /evidence="ECO:0000259|SMART:SM01185"
FT   DOMAIN          139..194
FT                   /note="Elongation factor P C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00841"
SQ   SEQUENCE   195 AA;  21830 MW;  022A7E2316C7A4B2 CRC64;
     MISMLGGRKL MINSTDFRTG LTIEIDGGVW QIVDFQHVKP GKGAAFVRTK IKNVETGAVV
     ERTFNPNEKM PAAHLETRNM QYLYEADGMY TFMDTESYEQ TELNKDQLGD ALNYLMENME
     VSLQTFKGRI IGISLPNSVN LKVTECEPSV KGNTATGATK MAKVETGYEV RVPLFVNEGD
     TLRIDTRTGN YIERA
//
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