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Database: UniProt
Entry: G9YKA1_9FIRM
LinkDB: G9YKA1_9FIRM
Original site: G9YKA1_9FIRM 
ID   G9YKA1_9FIRM            Unreviewed;       185 AA.
AC   G9YKA1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
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=HMPREF0080_02111 {ECO:0000313|EMBL:EHM37572.1};
OS   Anaeroglobus geminatus F0357.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Anaeroglobus.
OX   NCBI_TaxID=861450 {ECO:0000313|EMBL:EHM37572.1, ECO:0000313|Proteomes:UP000005481};
RN   [1] {ECO:0000313|EMBL:EHM37572.1, ECO:0000313|Proteomes:UP000005481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0357 {ECO:0000313|EMBL:EHM37572.1,
RC   ECO:0000313|Proteomes:UP000005481};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) 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:EHM37572.1}.
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DR   EMBL; AGCJ01000094; EHM37572.1; -; Genomic_DNA.
DR   RefSeq; WP_006791072.1; NZ_JH417616.1.
DR   AlphaFoldDB; G9YKA1; -.
DR   STRING; 861450.HMPREF0080_02111; -.
DR   GeneID; 85020132; -.
DR   PATRIC; fig|861450.3.peg.1934; -.
DR   eggNOG; COG0231; Bacteria.
DR   HOGENOM; CLU_074944_0_1_9; -.
DR   OrthoDB; 9801844at2; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000005481; 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:UP000005481}.
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;  20542 MW;  ED35AEE589EEA910 CRC64;
     MITSNDFRPG VTIEIDGQVW QVVEFQHVKP GKGAAFVRAK IKNLETGAVV ERTWNAGEKV
     QEGRVDRRQM QYLYESDGMY VFMDNESYEQ IELDKEALGS AVNFLKEEMN ASVMMFKGKV
     IGIDLPATVE LRVVETDPGI RGDTATGGSK PATLETGYVV KVPLFINEGE LLTIDTRTGQ
     YTGRA
//
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