IF3_LEPIN
ID IF3_LEPIN Reviewed; 179 AA.
AC Q8F6Q9;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Translation initiation factor IF-3 {ECO:0000255|HAMAP-Rule:MF_00080};
GN Name=infC {ECO:0000255|HAMAP-Rule:MF_00080}; OrderedLocusNames=LA_1242;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
CC -!- FUNCTION: IF-3 binds to the 30S ribosomal subunit and shifts the
CC equilibrum between 70S ribosomes and their 50S and 30S subunits in
CC favor of the free subunits, thus enhancing the availability of 30S
CC subunits on which protein synthesis initiation begins.
CC {ECO:0000255|HAMAP-Rule:MF_00080}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00080}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00080}.
CC -!- SIMILARITY: Belongs to the IF-3 family. {ECO:0000255|HAMAP-
CC Rule:MF_00080}.
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DR EMBL; AE010300; AAN48441.1; -; Genomic_DNA.
DR RefSeq; NP_711423.1; NC_004342.2.
DR RefSeq; WP_001189133.1; NC_004342.2.
DR AlphaFoldDB; Q8F6Q9; -.
DR SMR; Q8F6Q9; -.
DR STRING; 189518.LA_1242; -.
DR EnsemblBacteria; AAN48441; AAN48441; LA_1242.
DR GeneID; 61142340; -.
DR KEGG; lil:LA_1242; -.
DR PATRIC; fig|189518.3.peg.1243; -.
DR HOGENOM; CLU_054919_3_2_12; -.
DR InParanoid; Q8F6Q9; -.
DR OMA; RNMIMFL; -.
DR PRO; PR:Q8F6Q9; -.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR Gene3D; 3.10.20.80; -; 1.
DR Gene3D; 3.30.110.10; -; 1.
DR HAMAP; MF_00080; IF_3; 1.
DR InterPro; IPR036788; T_IF-3_C_sf.
DR InterPro; IPR036787; T_IF-3_N_sf.
DR InterPro; IPR019813; Translation_initiation_fac3_CS.
DR InterPro; IPR001288; Translation_initiation_fac_3.
DR InterPro; IPR019815; Translation_initiation_fac_3_C.
DR InterPro; IPR019814; Translation_initiation_fac_3_N.
DR PANTHER; PTHR10938; PTHR10938; 1.
DR Pfam; PF00707; IF3_C; 1.
DR Pfam; PF05198; IF3_N; 1.
DR SUPFAM; SSF54364; SSF54364; 1.
DR SUPFAM; SSF55200; SSF55200; 1.
DR TIGRFAMs; TIGR00168; infC; 1.
DR PROSITE; PS00938; IF3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..179
FT /note="Translation initiation factor IF-3"
FT /id="PRO_0000177535"
SQ SEQUENCE 179 AA; 20776 MW; 3C82FEDB3AB10AF9 CRC64;
MQRKPSQKSA TDKLFNHRVN EKITGVSRVR LVSDDGVAIV SFEEALRKAK EENLDLVEVS
ADQELHVCKI IDYGKYKFEL LKKSKEAKKK QHVINVKEIK IRPRIESHDY EIKKKHAQEF
LGKGDKVKVS LRFRGREMMH SDLGMKVVYR MIEDLKEHGT AERDPIQDGK QIVVIINPK