ID IF1_AERS4 Reviewed; 72 AA. AC A4SNL6; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 91. 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=ASA_2445; OS Aeromonas salmonicida (strain A449). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=382245; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A449; RX PubMed=18801193; DOI=10.1186/1471-2164-9-427; RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., RA Brown L.L.; RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into RT the evolution of a fish pathogen."; RL BMC Genomics 9:427-427(2008). CC -!- FUNCTION: One of the essential components for the initiation of protein CC synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit CC to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps CC modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). CC Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are CC released leaving the mature 70S translation initiation complex. CC {ECO:0000255|HAMAP-Rule:MF_00075}. CC -!- SUBUNIT: Component of the 30S ribosomal translation pre-initiation CC complex which assembles on the 30S ribosome in the order IF-2 and IF-3, CC IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at CC any time during PIC assembly. {ECO:0000255|HAMAP-Rule:MF_00075}. 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; CP000644; ABO90488.1; -; Genomic_DNA. DR RefSeq; WP_005300033.1; NC_009348.1. DR AlphaFoldDB; A4SNL6; -. DR SMR; A4SNL6; -. DR STRING; 29491.GCA_000820065_01481; -. DR GeneID; 83598855; -. DR KEGG; asa:ASA_2445; -. DR eggNOG; COG0361; Bacteria. DR HOGENOM; CLU_151267_1_0_6; -. DR Proteomes; UP000000225; 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; IPR003029; S1_domain. 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 SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS50832; S1_IF1_TYPE; 1. PE 3: Inferred from homology; KW Cytoplasm; Initiation factor; Protein biosynthesis; RNA-binding; KW rRNA-binding. FT CHAIN 1..72 FT /note="Translation initiation factor IF-1" FT /id="PRO_0000338755" FT DOMAIN 1..72 FT /note="S1-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00075" SQ SEQUENCE 72 AA; 8191 MW; 40BB60BB2BDA1FB8 CRC64; MAKEDSIEMQ GTILETLPNT MFRVELENGH VVIAHISGKM RKNYIRILTG DKVTVALTPY DLSKGRIVFR SR //