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Database: UniProt
Entry: E1IDC2_9CHLR
LinkDB: E1IDC2_9CHLR
Original site: E1IDC2_9CHLR 
ID   E1IDC2_9CHLR            Unreviewed;       278 AA.
AC   E1IDC2;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, 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=OSCT_1323 {ECO:0000313|EMBL:EFO80799.1};
OS   Oscillochloris trichoides DG-6.
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Oscillochloridaceae; Oscillochloris.
OX   NCBI_TaxID=765420 {ECO:0000313|EMBL:EFO80799.1, ECO:0000313|Proteomes:UP000054010};
RN   [1] {ECO:0000313|EMBL:EFO80799.1, ECO:0000313|Proteomes:UP000054010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG-6 {ECO:0000313|EMBL:EFO80799.1,
RC   ECO:0000313|Proteomes:UP000054010};
RX   PubMed=21037015; DOI=10.1128/JB.00931-10;
RA   Kuznetsov B.B., Ivanovsky R.N., Keppen O.I., Sukhacheva M.V.,
RA   Bumazhkin B.K., Patutina E.O., Beletsky A.V., Mardanov A.V., Baslerov R.V.,
RA   Panteleeva A.N., Kolganova T.V., Ravin N.V., Skryabin K.G.;
RT   "Draft genome sequence of the anoxygenic filamentous phototrophic bacterium
RT   Oscillochloris trichoides subsp. DG-6.";
RL   J. Bacteriol. 193:321-322(2011).
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   -!- 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:EFO80799.1}.
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DR   EMBL; ADVR01000040; EFO80799.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1IDC2; -.
DR   STRING; 765420.OSCT_1323; -.
DR   eggNOG; COG0231; Bacteria.
DR   HOGENOM; CLU_074944_0_0_0; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000054010; 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   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:UP000054010}.
FT   DOMAIN          158..214
FT                   /note="Translation elongation factor P/YeiP central"
FT                   /evidence="ECO:0000259|SMART:SM01185"
FT   DOMAIN          222..277
FT                   /note="Elongation factor P C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00841"
SQ   SEQUENCE   278 AA;  30651 MW;  A0EB4495F3775779 CRC64;
     MVTAAGSIQS YDHVLWLGAS MPIDMKLRLP AGVRGRLRLP EELFSLLLAA SPPTAEKKAG
     LGRTPNMGIY APNTDHMPSD EVDTRSFATM ASGTTSDLRT GIVLRYNNDL YQVVEFQHVA
     PGNWRAFVRM KLKNLNNGKV IEDRVRAGSD IEIVRIERRP MQFLYREGED FVFMDNSTYD
     QVQVGSAAVG AGARFLKENE NADLVYDAER EVLLGVELPI FVTLAVTETT IAVRGDTATN
     VTKPATLETG AVIQVPGFVN EGDVLKIDTR TGEYIERV
//
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