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Database: UniProt
Entry: F8L4N7_SIMNZ
LinkDB: F8L4N7_SIMNZ
Original site: F8L4N7_SIMNZ 
ID   F8L4N7_SIMNZ            Unreviewed;       188 AA.
AC   F8L4N7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Elongation factor P {ECO:0000256|HAMAP-Rule:MF_00141};
DE            Short=EF-P {ECO:0000256|HAMAP-Rule:MF_00141};
GN   Name=efp2 {ECO:0000313|EMBL:CCB88282.1};
GN   Synonyms=efp {ECO:0000256|HAMAP-Rule:MF_00141};
GN   OrderedLocusNames=SNE_A04050 {ECO:0000313|EMBL:CCB88282.1};
OS   Simkania negevensis (strain ATCC VR-1471 / Z).
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Simkaniaceae;
OC   Simkania.
OX   NCBI_TaxID=331113 {ECO:0000313|EMBL:CCB88282.1, ECO:0000313|Proteomes:UP000000496};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Z;
RA   Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA   Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA   Myers G.S.A., Horn M.;
RT   "Unity in variety -- the pan-genome of the Chlamydiae.";
RL   Mol. Biol. Evol. 0:0-0(2011).
RN   [2] {ECO:0000313|EMBL:CCB88282.1, ECO:0000313|Proteomes:UP000000496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1471 / Z {ECO:0000313|Proteomes:UP000000496};
RX   PubMed=21690563; DOI=10.1093/molbev/msr161;
RA   Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA   Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA   Myers G.S., Horn M.;
RT   "Unity in variety--the pan-genome of the Chlamydiae.";
RL   Mol. Biol. Evol. 28:3253-3270(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.
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}.
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DR   EMBL; FR872582; CCB88282.1; -; Genomic_DNA.
DR   RefSeq; WP_013942749.1; NC_015713.1.
DR   AlphaFoldDB; F8L4N7; -.
DR   STRING; 331113.SNE_A04050; -.
DR   KEGG; sng:SNE_A04050; -.
DR   eggNOG; COG0231; Bacteria.
DR   HOGENOM; CLU_074944_0_0_0; -.
DR   OrthoDB; 9801844at2; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000000496; Chromosome gsn.131.
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:UP000000496}.
FT   DOMAIN          69..123
FT                   /note="Translation elongation factor P/YeiP central"
FT                   /evidence="ECO:0000259|SMART:SM01185"
FT   DOMAIN          131..187
FT                   /note="Elongation factor P C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00841"
SQ   SEQUENCE   188 AA;  20889 MW;  4F577060024688AF CRC64;
     MAQVSTNEFK SGMKVEVDGD PYTIVNVEFV KPGKGQAFTR TKLKHLTSGR VVERTFRSGE
     KLDLADVEET KMRMLYREGT DVVFMHDETF DQLHVPLSAI GSTEAYLMEE TLYDLVLYKG
     TVVDVAPPTF MEMKITETSP GVKGDTASGR VLKPAITETG AKIQVPIFID EGEVVKVDTR
     TGEYVSRV
//
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