IF1_ECOLI
ID IF1_ECOLI Reviewed; 72 AA.
AC P69222; P02998;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
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=b0884, JW0867;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3037488; DOI=10.1093/nar/15.13.5157;
RA Sands J.F., Cummings H.S., Sacerdot C., Dondon L., Grunberg-Manago M.,
RA Hershey J.W.B.;
RT "Cloning and mapping of infA, the gene for protein synthesis initiation
RT factor IF1.";
RL Nucleic Acids Res. 15:5157-5168(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1909328; DOI=10.1016/s0021-9258(18)55327-8;
RA Cummings H.S., Sands J.F., Foreman P.C., Fraser J., Hershey J.W.B.;
RT "Structure and expression of the infA operon encoding translational
RT initiation factor IF1. Transcriptional control by growth rate.";
RL J. Biol. Chem. 266:16491-16498(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=8331068; DOI=10.1128/jb.175.14.4364-4374.1993;
RA Shrader T.E., Tobias J.W., Varshavsky A.;
RT "The N-end rule in Escherichia coli: cloning and analysis of the leucyl,
RT phenylalanyl-tRNA-protein transferase gene aat.";
RL J. Bacteriol. 175:4364-4374(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP PROTEIN SEQUENCE OF 2-72, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=MRE-600;
RX PubMed=376343; DOI=10.1016/0014-5793(79)81316-2;
RA Pon C.L., Wittmann-Liebold B., Gualerzi C.;
RT "Structure-function relationships in Escherichia coli initiation factors.
RT II. Elucidation of the primary structure of initiation factor IF-1.";
RL FEBS Lett. 101:157-160(1979).
RN [8]
RP PROTEIN SEQUENCE OF 2-11.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=22562136; DOI=10.1038/nsmb.2285;
RA Milon P., Maracci C., Filonava L., Gualerzi C.O., Rodnina M.V.;
RT "Real-time assembly landscape of bacterial 30S translation initiation
RT complex.";
RL Nat. Struct. Mol. Biol. 19:609-615(2012).
RN [10]
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 [11]
RP STRUCTURE BY NMR.
RX PubMed=9135158; DOI=10.1093/emboj/16.6.1436;
RA Sette M., van Tilborg P., Spurio R., Kaptein R., Paci M., Gualerzi C.O.,
RA Boelens R.;
RT "The structure of the translational initiation factor IF1 from E.coli
RT contains an oligomer-binding motif.";
RL EMBO J. 16:1436-1443(1997).
RN [12]
RP MODEL BY ELECTRON MICROSCOPY (18.3 ANGSTROMS), AND SUBUNIT.
RX PubMed=21750663; DOI=10.1371/journal.pbio.1001095;
RA Julian P., Milon P., Agirrezabala X., Lasso G., Gil D., Rodnina M.V.,
RA Valle M.;
RT "The cryo-EM structure of a complete 30S translation initiation complex
RT from Escherichia coli.";
RL PLoS Biol. 9:E1001095-E1001095(2011).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Binds in the vicinity of the A-site. Stabilizes the binding
CC of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-
CC tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding
CC the 30S pre-initiation complex (PIC). Upon addition of the 50S
CC ribosomal subunit, IF-1, IF-2 and IF-3 are released leaving the mature
CC 70S translation initiation complex. {ECO:0000269|PubMed:22562136,
CC ECO:0000269|PubMed:376343}.
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 ECO:0000269|PubMed:21750663, ECO:0000269|PubMed:22562136}.
CC -!- INTERACTION:
CC P69222; Q46864: mqsA; NbExp=2; IntAct=EBI-1120746, EBI-1120353;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00075,
CC ECO:0000269|PubMed:376343}.
CC -!- SIMILARITY: Belongs to the IF-1 family. {ECO:0000255|HAMAP-
CC Rule:MF_00075}.
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DR EMBL; Y00373; CAA68446.1; -; Genomic_DNA.
DR EMBL; M63145; AAC36912.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L10383; AAA03232.1; -; Unassigned_DNA.
DR EMBL; U00096; AAC73970.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35602.1; -; Genomic_DNA.
DR PIR; A27855; FIEC1.
DR RefSeq; NP_415404.1; NC_000913.3.
DR RefSeq; WP_001040187.1; NZ_STEB01000006.1.
DR PDB; 1AH9; NMR; -; A=2-72.
DR PDB; 1ZO1; EM; 13.80 A; W=2-70.
DR PDBsum; 1AH9; -.
DR PDBsum; 1ZO1; -.
DR AlphaFoldDB; P69222; -.
DR SMR; P69222; -.
DR BioGRID; 4262047; 51.
DR BioGRID; 849874; 3.
DR ComplexPortal; CPX-2244; Translation initiation factor complex.
DR DIP; DIP-48250N; -.
DR IntAct; P69222; 10.
DR STRING; 511145.b0884; -.
DR jPOST; P69222; -.
DR PaxDb; P69222; -.
DR PRIDE; P69222; -.
DR EnsemblBacteria; AAC73970; AAC73970; b0884.
DR EnsemblBacteria; BAA35602; BAA35602; BAA35602.
DR GeneID; 60371679; -.
DR GeneID; 64296173; -.
DR GeneID; 67414644; -.
DR GeneID; 945500; -.
DR KEGG; ecj:JW0867; -.
DR KEGG; eco:b0884; -.
DR PATRIC; fig|1411691.4.peg.1394; -.
DR EchoBASE; EB0499; -.
DR eggNOG; COG0361; Bacteria.
DR HOGENOM; CLU_151267_1_0_6; -.
DR InParanoid; P69222; -.
DR OMA; AHVSGKM; -.
DR PhylomeDB; P69222; -.
DR BioCyc; EcoCyc:EG10504-MON; -.
DR EvolutionaryTrace; P69222; -.
DR PRO; PR:P69222; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0043022; F:ribosome binding; IDA:EcoCyc.
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; -; 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; IPR022967; S1_dom.
DR InterPro; IPR004368; TIF_IF1.
DR PANTHER; PTHR33370; PTHR33370; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00008; infA; 1.
DR PROSITE; PS50832; S1_IF1_TYPE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Initiation factor;
KW Protein biosynthesis; Reference proteome; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:376343,
FT ECO:0000269|PubMed:9868784"
FT CHAIN 2..72
FT /note="Translation initiation factor IF-1"
FT /id="PRO_0000095785"
FT DOMAIN 2..72
FT /note="S1-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00075"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:1AH9"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:1AH9"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:1AH9"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1AH9"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1AH9"
SQ SEQUENCE 72 AA; 8250 MW; CDFE0845C4CBE147 CRC64;
MAKEDNIEMQ GTVLETLPNT MFRVELENGH VVTAHISGKM RKNYIRILTG DKVTVELTPY
DLSKGRIVFR SR
