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Database: UniProt
Entry: L0DN84_SINAD
LinkDB: L0DN84_SINAD
Original site: L0DN84_SINAD 
ID   L0DN84_SINAD            Unreviewed;       187 AA.
AC   L0DN84;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
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   OrderedLocusNames=Sinac_6200 {ECO:0000313|EMBL:AGA30298.1};
OS   Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS   MOB10).
OC   Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC   Singulisphaera.
OX   NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA30298.1, ECO:0000313|Proteomes:UP000010798};
RN   [1] {ECO:0000313|EMBL:AGA30298.1, ECO:0000313|Proteomes:UP000010798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC   {ECO:0000313|Proteomes:UP000010798};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
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|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; CP003364; AGA30298.1; -; Genomic_DNA.
DR   RefSeq; WP_015249384.1; NZ_JH621481.1.
DR   AlphaFoldDB; L0DN84; -.
DR   STRING; 886293.Sinac_6200; -.
DR   KEGG; saci:Sinac_6200; -.
DR   eggNOG; COG0231; Bacteria.
DR   HOGENOM; CLU_074944_0_1_0; -.
DR   OrthoDB; 9801844at2; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000010798; Chromosome.
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:SF14; EFP_N DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR30053; ELONGATION FACTOR P; 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:UP000010798}.
FT   DOMAIN          68..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   187 AA;  20966 MW;  193BAE4FC6CFC0E0 CRC64;
     MMIKATDIRR GMVITIEGTN FVVVDFAHHT PGNLRAMVQT KLRNMNSGAL IDKRLRSVDQ
     IEVPYVETKQ FEYLYSSGDE HVFMESETFD QLSFPPEILG TAMQYILPNS KVQVMYVDDK
     PVSVEVPASI DLTVADTPPS LKGATATNQY KEAILENGLK VQVPPFIGPG EKIRIDTRTG
     EYVERVK
//
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