ID IF1_THET8 Reviewed; 72 AA. AC Q5SHR1; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 107. DE RecName: Full=Translation initiation factor IF-1 {ECO:0000255|HAMAP-Rule:MF_00075}; GN Name=infA {ECO:0000255|HAMAP-Rule:MF_00075}; GN OrderedLocusNames=TTHA1669; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP REVIEW. RX PubMed=22515367; DOI=10.3109/10409238.2012.678284; RA Milon P., Rodnina M.V.; RT "Kinetic control of translation initiation in bacteria."; RL Crit. Rev. Biochem. Mol. Biol. 47:334-348(2012). RN [3] RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 2-72, FUNCTION, INTERACTION WITH RP S12, SUBUNIT, RIBOSOME-BINDING, AND RRNA-BINDING. RX PubMed=11228145; DOI=10.1126/science.1057766; RA Carter A.P., Clemons W.M. Jr., Brodersen D.E., Morgan-Warren R.J., RA Hartsch T., Wimberly B.T., Ramakrishnan V.; RT "Crystal structure of an initiation factor bound to the 30S ribosomal RT subunit."; RL Science 291:498-501(2001). CC -!- FUNCTION: One of the essential components for the initiation of protein CC synthesis. Binds in the vicinity of the A-site (PubMed:11228145). CC Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N- CC formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA CC selection, yielding the 30S pre-initiation complex (PIC). Upon addition CC of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving CC the mature 70S translation initiation complex. {ECO:0000255|HAMAP- CC Rule:MF_00075, ECO:0000269|PubMed:11228145}. CC -!- SUBUNIT: Binds to the 30S ribosomal subunit, contacting protein S12 and CC the 16S rRNA (PubMed:11228145). Component of the 30S ribosomal CC translation pre-initiation complex which assembles on the 30S ribosome CC in the order IF-2 and IF-3, IF-1 and N-formylmethionyl-tRNA(fMet); mRNA CC recruitment can occur at any time during PIC assembly. CC {ECO:0000255|HAMAP-Rule:MF_00075, ECO:0000269|PubMed:11228145}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00075}. CC -!- SIMILARITY: Belongs to the IF-1 family. {ECO:0000255|HAMAP- CC Rule:MF_00075}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP008226; BAD71492.1; -; Genomic_DNA. DR RefSeq; WP_008633373.1; NC_006461.1. DR RefSeq; YP_144935.1; NC_006461.1. DR PDB; 1HR0; X-ray; 3.20 A; W=2-72. DR PDB; 5LMN; EM; 3.55 A; W=1-72. DR PDB; 5LMO; EM; 4.30 A; W=1-72. DR PDB; 5LMP; EM; 5.35 A; W=1-72. DR PDB; 5LMQ; EM; 4.20 A; W=1-72. DR PDB; 5LMR; EM; 4.45 A; W=1-72. DR PDB; 5LMS; EM; 5.10 A; W=1-72. DR PDB; 5LMT; EM; 4.15 A; W=1-72. DR PDB; 5LMV; EM; 4.90 A; W=1-72. DR PDB; 5ME0; EM; 13.50 A; V=1-72. DR PDB; 5ME1; EM; 13.50 A; V=1-72. DR PDB; 6O7K; EM; 4.20 A; 5=2-72. DR PDBsum; 1HR0; -. DR PDBsum; 5LMN; -. DR PDBsum; 5LMO; -. DR PDBsum; 5LMP; -. DR PDBsum; 5LMQ; -. DR PDBsum; 5LMR; -. DR PDBsum; 5LMS; -. DR PDBsum; 5LMT; -. DR PDBsum; 5LMV; -. DR PDBsum; 5ME0; -. DR PDBsum; 5ME1; -. DR PDBsum; 6O7K; -. DR AlphaFoldDB; Q5SHR1; -. DR EMDB; EMD-2448; -. DR EMDB; EMD-3494; -. DR EMDB; EMD-3495; -. DR EMDB; EMD-4073; -. DR EMDB; EMD-4074; -. DR EMDB; EMD-4075; -. DR EMDB; EMD-4076; -. DR EMDB; EMD-4077; -. DR EMDB; EMD-4078; -. DR EMDB; EMD-4079; -. DR EMDB; EMD-4083; -. DR SMR; Q5SHR1; -. DR IntAct; Q5SHR1; 23. DR EnsemblBacteria; BAD71492; BAD71492; BAD71492. DR GeneID; 3168806; -. DR KEGG; ttj:TTHA1669; -. DR PATRIC; fig|300852.9.peg.1639; -. DR eggNOG; COG0361; Bacteria. DR HOGENOM; CLU_151267_1_0_0; -. DR PhylomeDB; Q5SHR1; -. DR EvolutionaryTrace; Q5SHR1; -. DR Proteomes; UP000000532; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule. DR CDD; cd04451; S1_IF1; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR HAMAP; MF_00075; IF_1; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR006196; RNA-binding_domain_S1_IF1. DR InterPro; IPR004368; TIF_IF1. DR NCBIfam; TIGR00008; infA; 1. DR PANTHER; PTHR33370; TRANSLATION INITIATION FACTOR IF-1, CHLOROPLASTIC; 1. DR PANTHER; PTHR33370:SF1; TRANSLATION INITIATION FACTOR IF-1, CHLOROPLASTIC; 1. DR Pfam; PF01176; eIF-1a; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS50832; S1_IF1_TYPE; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Initiation factor; Protein biosynthesis; KW Reference proteome; RNA-binding; rRNA-binding. FT CHAIN 1..72 FT /note="Translation initiation factor IF-1" FT /id="PRO_0000095893" FT DOMAIN 1..72 FT /note="S1-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00075" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:1HR0" FT TURN 19..21 FT /evidence="ECO:0007829|PDB:1HR0" FT STRAND 26..30 FT /evidence="ECO:0007829|PDB:1HR0" FT HELIX 39..43 FT /evidence="ECO:0007829|PDB:1HR0" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:1HR0" SQ SEQUENCE 72 AA; 8234 MW; 981E63B61223DDFC CRC64; MAKEKDTIRT EGVVTEALPN ATFRVKLDSG PEILAYISGK MRMHYIRILP GDRVVVEITP YDPTRGRIVY RK //